Ex Parte 8017376 et al

Patent Trial and Appeal Board

May 26, 2015

95001870 (P.T.A.B. May. 26, 2015)

UNITED STATES PATENT AND TRADEMARKOFFICE
UNITED STATES DEPARTMENT OF COMMERCE
United States Patent and Trademark Office
Address: COMMISSIONER FOR PATENTS
P.O. Box 1450
Alexandria, Virginia 22313-1450
www.uspto.gov
APPLICATION NO. FILING DATE FIRST NAMED INVENTOR ATTORNEY DOCKET NO. CONFIRMATION NO.
95/001,870 01/10/2012 8017376 GEVO-055/04US
310142-2306
2288
58249 7590 05/27/2015
COOLEY LLP
ATTN: Patent Group
1299 Pennsylvania Avenue, NW
Suite 700
Washington, DC 20004
EXAMINER
KUNZ, GARY L
ART UNIT PAPER NUMBER
3991
MAIL DATE DELIVERY MODE
05/27/2015 PAPER
Please find below and/or attached an Office communication concerning this application or proceeding.
The time period for reply, if any, is set in the attached communication.
PTOL-90A (Rev. 04/07)

UNITED STATES PATENT AND TRADEMARK OFFICE
____________

BEFORE PATENT TRIAL AND APPEAL BOARD
____________

BUTAMAX ADVANCED BIOFUELS, LLC
Requester and Appellant

v.

GEVO, INC.
Patent Owner and Respondent
____________

Appeal 2015-000179
Reexamination Control 95/001,870
Patent 8,017,376 B2
Technology Center 3900
____________

Before RICHARD M. LEBOVITZ, JEFFREY N. FREDMAN and
RAE LYNN P. GUEST, Administrative Patent Judges.

GUEST, Administrative Patent Judge.

DECISION ON APPEAL
The Requester appeals from the Patent Examiner’s decision not to
reject pending claims in the inter partes reexamination of U.S. Patent
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8,017,376 B2 (hereinafter the “’376 patent”).1 The Board’s jurisdiction for
this appeal is under 35 U.S.C. §§ 6(b), 134(c), and 315(b). We AFFIRM the
Examiner’s decision not to adopt Requester’s proposed rejections.

I. BACKGROUND
A request for inter partes reexamination under 35 U.S.C. §§ 311–318
and 37 C.F.R. §§ 1.902-1.997 for the ’376 patent was filed on January
13, 2012, by a Third-Party Requester, Butamax Advanced Biofuels, LLC
(hereinafter “Requester”). See Request for Inter Partes Reexamination 1
(hereinafter “Request”); Requester’s Appeal Brief, dated May 2, 2014
(hereinafter “Req. App. Br.”). The Patent Owner and Respondent is Gevo,
Inc. (hereinafter “Patent Owner”). Patent Owner’s Respondent Brief, dated
June 2, 2014 (hereinafter “PO Res. Br.”).
The ’376 patent is the subject of a litigation proceeding in the United
States District Court for the Eastern District of Delaware styled Gevo Inc. v.
Butamax Adv. Biofuels LLC, 1-13-cv-00576, in which judgment on
non-infringement was been entered. No determination has been made
regarding the validity of claim 9 of the ’376 patent. See PO Res. Br., Exhibit
15, Memorandum Opinion 38 (denying summary judgment on the issue of
validity of the ’376 patent); see also id., Exhibit 16, Final Judgment
(acknowledging the dismissal of claims and counterclaims relating to the
invalidity and/or enforceability of the ’376 patent). A related patent, US

1 The ’376 patent issued September 13, 2011, to Catherine Asleson Dundon,
et al.
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8,273,565, was cancelled pursuant to an Inter Partes Review IPR2013-
00539 on March 4, 2014 (Paper 9).
An oral hearing was scheduled for March 18, 2015. However, the
parties subsequently waived oral hearing. See Withdrawal from Attendance
at Oral Hearing, filed February 5, 2015. Accordingly, this case has been
decided entirely on the briefs of record.
The ’376 patent is directed to recombinant yeast microorganisms (e.g.,
S. cerevisiae) that have improved DHAD (dihydroxy acid dehydratase)
activity. DHAD is an enzyme that catalyzes the conversions of 2,3-
dihydroxyisovalerate to α-ketoisovalerate and of 2,3-dihydroxy-3-
methylvalerate to 2-keto-3-methylvalerate. ’376 patent, col. 1, ll. 45–60.
These reactions are important in the biosynthetic pathways that allow certain
microorganisms to produce desirable products, such as valine, isoleucine,
leucine, pantothenic acid (vitamin B5), and isobutanol, which can be used as
a biofuel. Id. at col. 1, l. 45 to col. 2, l. 16.
The ’376 patent was issued with original claims 1–20. During
reexamination, Patent Owner cancelled claims 1, 10, 13, and 15. The
remaining claims were amended to incorporate the subject matter of claim 9.
Claim 9 depended from canceled claim 1. Accordingly, the Examiner
interpreted the amendments such that “claim 9 now contains all of the
subject matter of claim 1.” See Right of Appeal Notice dated January 17,
2014 (“RAN”) 4. Claims 2–9, 11, 12, 14, and 16–20 were subsequently
confirmed by the Examiner as patentable. Id. Requester appeals the
non-adoption of the following proposed rejections. Req. App. Br. 2.
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1. Claims 2–9, 11, 12, 14, and 17–20 under 35 U.S.C. § 102(e)2 as
anticipated by Flint (WO 2011/103300 A2, published August 25,
2011);
2. Claims 2–9, 11, and 18–20 under 35 U.S.C. § 102(e) as anticipated
by Urano (US 2011/0076733 A1, published March 31, 2011);
3. Claims 2–4, 6–9, 11, 12, 14, and 16–20 under 35 U.S.C. § 103(a) as
obvious over Anthony (US 2010/0081179 A1, published April 1,
2010) in view of Puig;3 and
4. Claim 5 under 35 U.S.C. § 103(a) as obvious over Anthony in view
of Puig and Li (US 2009/0163376 A1, published June 25, 2009).
Claim 9, the sole independent claims in this appeal, is representative.
Claim 9 and cancelled claim 1 from which it depends read as follows:
1. (cancelled) A recombinant yeast microorganism
comprising a recombinantly overexpressed polynucleotide
encoding a dihydroxy acid dehydratase (DHAD), and
recombinantly overexpressed one or more polynucleotides
encoding one or more activator of ferrous transport (Aft)
proteins which increase the dehydratase activity of DHAD

9. The recombinant yeast microorganism of claim 1,
wherein said DHAD is localized in the cytosol.
REJECTIONS BASED ON FLINT AND URANO
The Examiner did not adopt the rejections based on Flint and Urano
under 35 U.S.C. § 102(e) because the Examiner granted claim 9 of the ’376

2 All references to U.S. statutes are as written prior to the Leahy-Smith
America Invents Act, signed into law on September 16, 2011. See AIA
§ 6(c)(3)(C) (2011).
3 S. Puig, et al., “Coordinated Remodeling of Cellular Metabolism during
Iron Deficiency through Targeted mRNA Degradation,” Cell, 120:99–110
(January 14, 2005).
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patent, the benefit of priority to U.S. provisional application number
61/263,952, filed November 24, 2009 (hereinafter “the ’952 provisional
application”). RAN 5, 12-14. Accordingly, the Examiner determined that
the priority date of the ’376 patent antedates the earliest filing date of Flint
(US App. 61/305,333, filed February 17, 2010). The Examiner found that
Urano was not entitled to the filing dates of provisional applications
61/272,058, filed August 12, 2009, and 61/272,059, also filed August 12,
2009. Id. at 13-14. Thus, the Examiner found that the priority date of the
’376 patent antedates the earliest filing date to which Urano is entitled (US
App. 12/855,276, filed August 12, 2010). Requester does not contest the
Examiner’s determination that Urano is not entitled to an earlier priority
date. See generally Req. App. Br.
Requester initially contends that the claims of the ’376 patent have a
broad scope and are not meaningfully narrowed by the amendments. Req.
App. Br. 6–7. Requester argues that claims 2–4 and 6–8 merely recite
limitations that are “inherent to native yeast microorganisms,” such as the
isobutanol pathway recited in claim 2. Id.
We are not persuaded by Requester’s argument because all of the
claims still depend from claim 9, which depends from canceled claim 1
directed to a recombinant yeast microorganism. See RAN 4. Thus, the
claims are not directed to any native yeast microorganism, but to
recombinant microorganisms having increased DHAD activity. Thus, the
additional claims that are said to recite properties of native yeast merely
recite that these properties are also present in the recombinant
microorganism, and are not eliminated by the genetic modification, even to
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the extent that other non-recited features of native yeast may not be present
in the recombinant microorganism.
Requester further argues that the Examiner erred in awarding priority
of the ’376 patent claims to the ’952 provisional application because the
’952 provisional application allegedly does not describe and enable the full
scope of the amended claims. Req. App. Br. 7–13. In particular, Requester
contends that the description in the ’952 provisional application is prophetic
in nature and does not explicitly describe “a sequence for any particular Aft
protein that increases dehydratase activity of DHAD” or “a yeast strain
recombinantly overexpressing cytosolic DHAD and an Aft protein which
increases the activity of DHAD.” Id. at 9. According to the Requester and
supporting declarant, Dr. Theile,4 enabling support in the ’952 provisional
application would have had to disclose “(1) a sequence of a particular Aft
protein that increase dehydratase activity of a cytosolic DHAD; (2) a
specific yeast strain in which recombinant Aft expression increases the
dehydratase activity of DHAD; or (3) a specific vector that expresses Aft at
a level required for increasing the dehydratase activity of a DHAD.” Id. at
12 (citing First Thiele Decl. ¶¶ 34, 35, 41 and 42 and Second Thiele Decl. ¶
5–8 and 13–14). Requester argues that “it [is] unpredictable which Aft
protein to express in which yeast cell in order to achieve the claimed
increase in dehydratase activity of DHAD.” Id.

4 Dr. Dennis J. Thiele testifies to having 27 years of “significant training and
experience in the fields of molecular biology and yeast genetics,” including
an emphasis and substantial publications in the area of “metal homeostasis in
yeast” and an “understanding the regulation of iron and copper homeostasis
in yeast.” First Thiele Decl. ¶ 5 and ¶ 9. Dr. Thiele is also an author of
Puig, which is applied in this case. Id. ¶ 10.
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The ’952 provisional application describes that
Increasing the expression of the genes AFT1, AFT2, GRX3
and/or GRX4 alone or in combination will modulate the amount
and availability of iron in the yeast cytosol or
mitochondria. . . . Since Aft1 activates the expression of target
genes in response to changes in iron availability.[sic]
Overexpression of AFT1 is predicted to increase the machinery
to import more iron into the cytosol. In one embodiment, AFT1
is overexpressed from a plasmid or by inserting multiple copies
of the gene into the chromosome under the control of a
constitutive promoter. In another embodiment, native Aft1 is
replaced with a mutant version . . . Likewise, AFT2 is predicted
to result in increased expression of the machinery to import
more iron into the mitochondria. In one embodiment. AFT2 is
overexpressed from a plasmid or by inserting multlple copies of
the gene into the chromosome under the control of a
constitutive promoter. in another embodiment, native AFT2 is
replaced with a mutant version.
’952 application ¶ 154. In other words, the ’952 provisional application
describes that DHAD activity can be increased by the overexpression of the
gene that encodes the native Aft1 and Aft2 proteins. The ’952 provisional
application further hypothesizes on why overexpression of genes encoding
the Aft proteins provides this function:
Increase in iron in either the cytosol or the mitochondria by this
method may make iron more available for use in FeS
cluster-containing proteins, such as DHAD. An increase in iron
may lead to a corresponding increase in DHAD activity. An
increase in DHAD activity in the yeast cytosol, in the context of
an isobutanol production pathway, may lead to an increase in
isobutanol productivity, titer, and/or yield by the cell.
Id. ¶ 154. The ’952 provisional application further describes that native Aft1
protein can be replaced with a mutant version that is constitutively active via
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a conserved cysteine-to-phenylalanine mutation. Id. ¶ 154. The ’952
provisional application further describes that “mutant strains carrying the
AFT1-1 UP allele exhibit a gain-of-function phenotype in which iron uptake
cannot be repressed by available iron in the environment.” Id. ¶ 150. The
’952 provisional application further describes that “proteins having a
homology to any one of AFT1, AFT2, GRX3, and GRX3 of at least about
70%, at least about 80% or at least about 90% similarity can be used for a
similar purpose.” Id. ¶ 158 and ¶ 223-228. Accordingly, we find that the
’952 provisional application provides sufficient written descriptive and
enabling support for one of ordinary skill in the art to understand that native
Aft1 or Aft2 proteins, proteins having 70% or more homology to native Aft1
or Aft2 proteins, or mutant proteins that are constituently active, all are
described as proteins that increase DHAD activity when genes encoding
these proteins are overexpressed in a yeast cell. Requester confirmed that
the particular sequences for native S. cerevisiae Aft1 and Aft2 proteins
(SEQ ID NO:2 and SEQ ID NO:4) were known in the art at the time of the
invention. Req. App. Br. 23; Second Thiele Decl. ¶ 22. Thus, the skilled
artisan would have recognized proteins within the described homology and
those with a conserved cysteine-to-phenylalanine mutation.
Dr. Thiele also argued that there was no discussion in the ’952
application of a genus of Aft proteins that, when overexpressed, would lead
to increased DHAD activity. See, e.g., First Thiele Decl. ¶ 35; Regents of
Univ. of Cal. v. Eli Lilly & Co., 119 F.3d 1559, 1568-1569 (Fed. Cir. 1997).
However, as indicated above, the sequence of Aft proteins, including
mutations of it, were known in the art at the time of the invention to be
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transcriptional factors and to possess regulatory transcriptional activity as
“activators of ferrous transport.” ’952 application ¶ 150-151. Thus, the
claimed genus of activators of ferrous transport are not new, as they were in
Eli Lilly, but instead were known proteins with a known activity that
Appellants in this case have put to a new use in increasing dehydratase
activity of DHAD by its known activity to do so. See, e.g., Capon v.
Eshhar, 418 F.3d 1349, (Fed. Cir. 2005) (“Both Eshhar and Capon explain
that this invention does not concern the discovery of gene function or
structure, as in Lilly. The chimeric genes here at issue are prepared from
known DNA sequences of known function. The Board’s requirement that
these sequences must be analyzed and reported in the specification does not
add descriptive substance. The Board erred in holding that the specifications
do not meet the written description requirement because they do not reiterate
the structure or formula or chemical name for the nucleotide sequences of
the claimed chimeric genes.)
Moreover, the ’952 provisional application describes AFT1-1up alleles
were known in the art at the time of the invention, a finding which is
supported by the teachings of Puig. See Puig, p. 109, col. 1, first full ¶
(“Plasmids containing AFT1-1up or AFT2-1up mutant alleles were a generous
gift from Dr. D. Winge.”). The ’952 provisional application further states
that overexpression may be accomplished by use of known plasmid vectors
or from single or multiple copy integration into the chromosomes using
known constitutive promoters, “such as TDN3, TEF1, CCW12, PGK1, and
ENO2”, the PDC1 promoter (a promoter from one of the glycolytic genes, or
a promoter from one of the ADH genes. The ’952 application ¶ 159. The
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’952 provisional application further states that “[m]ethods for
overexpressing a polypeptide from a native or heterologous nucleic acid
molecule are well known,” including the use of a regulatory element that
promotes the expression of the nucleic acid sequence that encodes the
desired protein. Id. ¶ 267. The ’952 provisional application also describes
the use of single or low copy centromeric plasmids. Id. The ’952
provisional application further describes a variety of yeast strains that could
be so modified. Id. ¶¶ 240–255.
Accordingly, the ’952 provisional application provides sufficient
support for the ordinary artisan to have arrived at the claimed overexpression
in a variety of well-known ways, such as via plasmid vectors including, for
example, AFT1-1up alleles, using constitutive promoters, or the presence of
multiple copies of a gene encoding Aft1 or Aft2 proteins. We find this
sufficient evidence that would have directed to the skilled artisan to have
overexpressed Aft proteins.
Moreover, the ’952 application describes methods for detecting
DHAD activity, namely by measuring ketoisovalerate generation via HPLC
from fractionated lysates of S. cerevisiae. See e.g., id. at ¶¶ 289, 319, 338,
358.
In determining whether experimentation is undue, we look to a
number of factors to consider: “(1) the quantity of experimentation
necessary, (2) the amount of direction or guidance presented, (3) the
presence or absence of working examples, (4) the nature of the invention,
(5) the state of the prior art, (6) the relative skill of those in the art, (7) the
predictability or unpredictability of the art, and (8) the breadth of the
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claims.” In re Wands, 858 F.2d 731, 737 (Fed. Cir.1988) (citing Ex Parte
Forman, 230 U.S.P.Q. 546, 547 (B.P.A.I.1986)). We are not persuaded of a
lack of enablement or undue experimentation in the disclosure of the ’952
provisional application merely due to the lack of specific examples of an
increase in DHAD activity with AFT1 or AFT2 overexpression or the fact
that some vectors did not work, as discussed in the ’209 provisional
application.5 See Req. App. Br. 10 and 12–13; see also First Thiele Decl. ¶
42. “[A] patent does not need to guarantee that the invention works for a
claim to be enabled. It is well settled that an invention may be patented
before it is actually reduced to practice. Similarly, a patentee is not required
to provide actual working examples; we have rejected enablement
challenges based on the theory that there can be no guarantee that prophetic
examples actually work.” Alcon Research Ltd. v. Barr Laboratories, Inc.,
745 F.3d 1180, 1189–90 (Fed. Cir. 2014) (internal citation omitted).
Moreover, Requester has not provided sufficient evidence that one of
ordinary skill in the art would have doubted that Aft overexpression would
have worked to increase DHAD activity at the time of the invention. See
Rasmusson v. SmithKline Beecham Corp., 413 F.3d 1318, 1324 (Fed. Cir.
2005) (requiring enabling support of the “utility as a drug, medicant, and the
like in human therapy” in response to substantial evidence that the skilled
artisan would not have believed that the recited compound was effective for

5 The ’376 patent also claims priority to US provisional application
61/350,209, filed June 1, 2010. The Examiner found that the ’376 patent
was also entitled to priority to the ’209 application. However, since priority
to the earlier filed ’952 provisional application is sufficient to antedate Flint
and Urano, we do not need to also address the ’209 application.
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treatment in humans); In re Brana, 51 F.3d 1560, 1566 (Fed. Cir. 1995)
(“[A] specification disclosure which contains a teaching of the manner and
process of making and using the invention ... must be taken as in compliance
with the enabling requirement of the first paragraph of § 112 unless there is
reason to doubt the objective truth of the statements contained therein which
must be relied on for enabling support.”).
Requester’s evidence, in view of the Wands factors, is not persuasive
of undue experimentation. To the contrary, we find that the guidance
provided by the ’952 provisional application is substantial and the relative
skill of those in the art to be high. Thus, we agree with the Patent Owner
that it would have been no more than routine experimentation and routine
optimization to determine which particular vectors, promotors, and yeast
strains would have been the most successful for overexpressing genes that
encode Aft proteins and, thus, increasing DHAD activity.
Accordingly, we agree with the Examiner’s finding that the claims of
the ’376 patent are entitled to a priority date of the ’952 provisional
application. Thus, the ’376 patent antedates the earliest dates entitled to
Flint and Urano, removing Flint and Urano as prior art references under
35 U.S.C. § 102(e).

REJECTIONS BASED ON ANTHONY AND PUIG
Claims 2–4, 6–9, 11, 12, 14, and 16–20 stand rejected under
35 U.S.C. § 103(a) as obvious over Anthony and Puig. Claim 5 stands
rejected under 35 U.S.C. § 103(a) as being unpatentable over Anthony and
Puig and further in view of Li.
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Anthony teaches a recombinant yeast cell that overexpresses a gene
that encodes for DHAD and increases DHAD activity by deleting a selection
of genes that encode proteins, such as LEU1 and ILV3 proteins, that
compete with DHAD for available Fe-S clusters. See Anthony ¶¶ 6–9, 74–
79 and 151–156. Anthony does not teach overexpressing a gene that
encodes Aft proteins.
Puig describes that, upon iron deprivation in yeast, transcription
factors Aft1 and Aft2 induce expression of the so called iron regulon, which
includes proteins involved in iron reduction at the plasma membrane, iron
uptake, iron mobilization from intracellular stores, and utilization from
heme, among others. Puig, p. 99, col. 2, first ¶. Puig thus measured the
growth under low iron conditions of Cth2-deletion yeast mutants as
compared to wild-type yeast cells, which use Cth2 to regulate mRNA that
are involved in iron dependent processes and create less competition for
iron-critical processes in low iron conditions. Id. at p. 100, col. 2, first full ¶.
Puig further studied Cth2 function during iron deficiency. See generally id.
Puig further teaches that “The Activation of CTH2 Transcription by Fe
Depletion Depends on Two Aft1 Binding Sites in the CTH2 Upstream
Sequence.” See Puig Suppl. Fig. S2,6 p. 100, ¶ spanning col. 1–2. It appears
that Puig used “[p]lasmids containing AFT1-1up or AFT2-1up mutant alleles”
available from Dr. Winge of the University of Utah. Id. at p. 109, col. 1,
first full ¶.

6 Supplemental Data for the Puig articles published in Cell can be accessed
online at http://www. cell.com/supplemental/S0092-8674(04)01100-6, as of
May 8, 2015.
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Requester contends that “a POSA having the acknowledged
motivation to activate Aft controlled iron regulation to affect Fe-dependent
processes, such as the activity of a recombinant DHAD protein, would have
been motivated to turn on the iron regulatory pathway by expressing an Aft
protein, instead of trying to activate only a single Aft controlled gene, such
as Cth2.” Req. App. Br. 25.
Patent Owner argues that, considering the desire to degrade certain
Fe-S cluster proteins, as taught by Anthony, the skilled artisan would have
considered it redundant to overexpress Aft proteins, when the results would
have been more efficiently met by overexpressing Cth2 proteins. PO Res.
Br. 9–10.
We find no persuasive evidence that a skilled artisan would have
expected an increase in cytosol DHAD activity in yeast cells by activating
the iron regulon. Puig describes that during iron depletion, Aft1 binds to
two sites in the CTH2 upstream sequence, which activates the transcription
of Cth2. Puig Suppl. Fig. S2. In particular, Puig found these two binding
sites similarly affected CTH2 expression in CM3260 wild-type and aft2
yeast cells in low iron conditions and in SPY145 yeast cells expressing
AFT1-1up or AFT1-2up. Id. Further Puig lists various endogenous proteins
downregulated or upregulated in iron deficient conditions. Id. at 103–104,
Table I; Suppl. Table S2 and Suppl. Table S3. Puig is silent as to the effect
of Cth2 on heterologous DHAD transcription. However, Puig identifies
endogenous DHAD (ILV3) as one of 84 endogenous genes that were
significantly upregulated in the absence of CTH2, including 45 Fe-related
genes. Id. at p. 101, col. 2, first full ¶, Table 1. Puig also indicates that
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“potentially other as yet uncharacterized pathways” could be downregulated
“in yeast under conditions of Fe deficiency.” See id. p. 101, col. 2, first
full ¶. While Anthony teaches only the targeting of certain genes encoding
specific Fe-S cluster proteins for deletion, such that heterologous DHAD is
unaffected, Puig’s deregulation activity by Cth2 is not so targeted.
Requester has not provided sufficient evidence that the skilled artisan would
have expected heterologous DHAD to be unaffected by Cth2-dependent
mRNA downregulation in the same manner that endogenous DHAD is
targeted for downregulation in iron-deficient conditions. To the contrary,
based on the teaching of Puig, the skilled artisan would expect Cth2 to target
heterologous RNA directed to iron related functions for degradation as it
does endogenous RNA. Moreover, Puig only describes the identified
downregulation as occurring in low iron conditions. Anthony describes that
DHAD activity relies on Fe-S clusters and, thus, relies on the presence or
even abundance of iron for increasing DHAD activity. Accordingly, the
skilled artisan would not have expected an increase in DHAD activity under
low iron conditions necessary to downregulate the competitive Fe-S cluster
proteins as taught by Puig.
Accordingly, we agree with the Patent Owner and the Examiner that
Requester’s contention reviews the teachings of Anthony and Puig with the
hindsight knowledge provided by the ’376 patent that the Aft1/2 iron
regulon increases cytosol DHAD activity in yeast cells by increasing iron
uptake in the cytosol. Accordingly, the claims of the ’376 patent are not
obvious under 35 U.S.C. § 103(a) in view of the teachings of Anthony and
Puig.
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SUMMARY
For the reasons discussed above, we affirm the Examiner’s decision
not to adopt any of the following proposed rejections:
1. Claims 2–9, 11, 12, 14, and 17–20 under 35 U.S.C. § 102(e) as
anticipated by Flint;
2. Claims 2–9, 11, and 18–20 under 35 U.S.C. § 102(e) as anticipated
by Urano;
3. Claims 2–4, 6–9, 11, 12, 14, and 16–20 under 35 U.S.C. § 103(a) as
unpatentable over Anthony in view of Puig; and
4. Claim 5 under 35 U.S.C. § 103(a) as unpatentable over Anthony in
view of Puig and Li.

In the event neither party files a request for rehearing within the time
provided in 37 C.F.R. § 41.79, and this decision becomes final and
appealable under 37 C.F.R. § 41.81, a party seeking judicial review must
timely serve notice on the Director of the United States Patent and
Trademark Office. See 37 C.F.R. §§ 90.1 and 1.983.

AFFIRMED

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PATENT OWNER:

COOLEY LLP
ATTN: Patent Group
1299 Pennsylvania Avenue, NW
Suite 700
Washington, DC 20004

THIRD-PARTY REQUESTER:

STERNE, KESSLER, GOLDSTEIN
& FOX P.L.L.C.
1100 New York Ave
Washington, DC 20005