We are using
molecular genetic approaches to elucidate functions
of indole-3-butyric acid (IBA) in Arabidopsis. Although
IBA is a naturally occurring form of the plant growth
hormone auxin and is used commercially to promote rooting
in many species, the molecular mechanisms by which it
acts are only beginning to be understood.
We have isolated IBA-response (ibr) mutants; some of these mutants have b-oxidation and peroxisome biogenesis defects. Our analysis suggests that IBA is converted into indole-3-acetic acid (IAA) using reactions analogous to those of fatty acid catabolism (b-oxidation), a largely peroxisomal process in plants. Thus these mutants are contributing to our understanding of plant peroxisomes and the genes necessary for their biogenesis.

To understand
auxin action, the functional significance of the endogenous
auxins must be determined. Identifying genes involved
in converting IBA to IAA is a prerequisite to understanding
the regulation and importance of this conversion.
This knowledge is essential to determine the contributions
of IBA relative to other inputs to the active auxin pool,
including de novo synthesis and conjugate hydrolysis.
In addition, elucidating the molecular mechanisms of IBA
action in a genetically tractable plant may provide insights
for agricultural IBA uses. For example, identifying
and characterizing the specific isozymes that convert
IBA to IAA may facilitate their modification in difficult-to-root
cultivars where IBA application is normally ineffective.
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pxa1 is an IBA response mutant; it elongates its primary root on inhibitory concentrations of IBA, but is resistant to the stimulatory effects of IBA on lateral root formation. pxa1 is defective in a peroxisomal transporter (Zolman et al., 2001).
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Lab members with IBA projects:
Post Docs:
Matthew Lingard
Lucia Strader
Graduate Students:
Naxhiely Martinez
Sarah Ratzel
Undergraduates:
Nicky Mehtani
Chaya Murali
Karie Runcie
Former Grad Students: A. Raquel Adham (Ph.D., 2005)
Melanie Monroe-Augustus
(Ph.D., 2004)
Andrew Woodward
(Ph.D., 2005)
Bethany Zolman (Ph.D., 2002)
We gratefully acknowledge support
for this research from the National Science Foundation
(IBN-0315596 and MCB 0745122), the Robert A. Welch Foundation,
predoctoral NIH fellowships (ARA and NM), a NIH training grant
(T32-GM08362; MMA and JR), and Houston Livestock Show
and Rodeo scholarships (ARA, AWW, EP, SR, MMA).
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Peroxisome-associated matrix protein degradation in Arabidopsis.
Lingard, M.J., Monroe-Augustus, M., and Bartel, B. (2009) Proc. Natl. Acad. Sci. USA (in press).
Disruption of ArabidopsisCHY1 reveals an important role of metabolic status in plant cold stress signaling.
Dong, C.-H., Zolman, B.K., Bartel, B., Lee, B.-h., Stevenson, B., Agarwal, M., and Zhu, J.-K. (2009) Molecular Plant 2, 59-72.
Abstract; full text; PDF
Arabidopsis iba response5 (ibr5) suppressors separate responses to various hormones.
Strader, L.C., Monroe-Augustus, M., Rogers, K.C., Lin, G.L., and Bartel, B. (2008) Genetics180, 2019-2031.
Abstract; full text; PDF
Identification and characterization of Arabidopsis indole-3-butyric acid response mutants defective in novel peroxisomal enzymes.
Zolman, B.K., Martinez, N., Millius, A., Adham, A.R., and Bartel, B. (2008) Genetics 180, 237-251.
Abstract; full text; PDF
IBR3, a novel peroxisomal acyl-CoA dehydrogenase-like protein required for indole-3-butyric acid response.
Zolman, B.K., Nyberg, M., and Bartel, B. (2007) Plant Molecular Biology 64, 59-72.
Abstract; full text; PDF
Identification and functional characterization of Arabidopsis PEROXIN4 and the interacting protein PEROXIN22.
Zolman, B.K., Monroe-Augustus, M., Silva, I.D., and Bartel, B. (2005) Plant Cell 17, 3422-3435.
Abstract; full text
Auxin: regulation, action, and interaction.
Woodward, A.W. and Bartel, B. (2005) Annals of Botany,95, 707-735.
Abstract; full text
Mutations in Arabidopsis thaliana acyl-CoA oxidase genes reveal overlapping and distinct roles in b-oxidation.
Adham, A.R., Zolman, B.K., Millius, A., and Bartel, B. (2005) The Plant Journal 41, 859-874.
Abstract; full text
The Arabidopsis peroxisomal targeting signal type 2 receptor PEX7 is necessary for peroxisome function and dependent on PEX5.
Woodward, A.W. and Bartel, B. (2005) Molecular Biology of the Cell 16, 573-583.
Abstract; full text
An
Arabidopsis indole-3-butyric acid-response mutant defective
in PEROXIN6, an apparent ATPase implicated in peroxisomal function.
Zolman, B.K. and Bartel, B. (2004) Proc.
Natl. Acad. Sci. USA 101, 1786-1791.
Abstract;
PDF
The
Arabidopsis pxa1 mutant is defective in an ATP-binding
cassette transporter-like protein required for peroxisomal fatty
acid b-oxidation.
Zolman, B.K., Silva, I.D., and Bartel, B.
(2001) Plant Physiology 127, 595-604. (On the cover)
Abstract;
full
text; PDF
chy1,
an Arabidopsis mutant with impaired b-oxidation, is defective
in a peroxisomal b-hydroxyisobutyryl-CoA hydrolase.
Zolman, B.K., Monroe-Augustus, M., Thompson,
B., Hawes, J.W., Krukenberg, K.A., Matsuda, S.P.T., and Bartel,
B. (2001) Journal of Biological Chemistry 276, 31037-31046.
Abstract;
full
text; PDF
Inputs
to the active indole-3-acetic acid pool: de novo synthesis,
conjugate hydrolysis, and indole-3-butyric acid b-oxidation.
Bartel, B., LeClere, S., Magidin, M., and
Zolman, B.K. (2001) Journal of Plant Growth Regulation 20, 198-216. (Review Article)
Abstract;
full
text
Genetic
analysis of indole-3-butyric acid responses in Arabidopsis
thaliana reveals four mutant classes.
Zolman, B.K, Yoder, A., and Bartel, B. (2000) Genetics 156, 1323-1337.
Abstract;
full
text; PDF
Links:
AraPerox
- Database of Putative Arabidopsis Peroxisomal Proteins
TAIR - The
Arabidopsis Information Resource
T-DNA Express
at the Salk Institute (insertion lines)
American Society of Plant Biologists
(Plant Cell, Plant
Physiology)
Center for Plant
Science at Rice University
Biochemistry and Cell Biology
Department
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