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Genetic analyses of the roles of peroxisomes and the
auxin indole-3-butyric acid (IBA) in Arabidopsis

Bonnie Bartel, Professor
Department of Biochemistry and Cell Biology
bartel@rice.edu

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.

 


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).

 

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).

Publications on IBA and peroxisomes:

Other Bartel lab projects:
Auxin signaling, conjugates, peroxisomes
triterpenes, IBA


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


Biochemistry