Award Abstract #0091826
Arabidopsis 2010: Plant Peroxisomal Biogenesis: Sorting/Function of Membrane Proteins and Peroxins

NSF Org:	MCB Division of Molecular and Cellular Biosciences
Initial Amendment Date:	April 12, 2001
Latest Amendment Date:	July 16, 2003
Award Number:	0091826
Award Instrument:	Continuing grant
Program Manager:	Eve Ida Barak MCB Division of Molecular and Cellular Biosciences BIO Directorate for Biological Sciences
Start Date:	April 15, 2001
Expires:	March 31, 2007 (Estimated)
Awarded Amount to Date:	$788828
Investigator(s):	Richard Trelease TRELEASE.DICK@ASU.EDU (Principal Investigator)
Sponsor:	Arizona State University ORSPA TEMPE, AZ 85287 480/965-5479
NSF Program(s):	CELLULAR ORGANIZATION, CELLULAR SYSTEMS, INSTRUMENTAT & INSTRUMENT DEVP
Field Application(s):
Program Reference Code(s):	SMET, BIOT, 9251, 9178, 9109, 1684, 1132, 1108
Program Element Code(s):	1132, 1114, 1108

ABSTRACT



Title: "Arabidopsis 2010: Plant Peroxisomal Biogenesis - Sorting/Function of Membrane Proteins and Peroxins".

Peroxisomes are ubiquitous subcellular organelles that possess a diverse array of enzymes and other protein contents that vary with developmental stage, and in response to environmental cues. The overall goal of this project is to identify Arabidopsis genes coding for peroxisomal membrane proteins (PMPs) involved in the biogenesis and functioning of peroxisomes, and then determine the specific function of the gene products. "Peroxin" genes code for a set of proteins (peroxins) that participate specifically in peroxisomal biogenesis (organelle replication and differentiation). Most peroxins are PMPs. To date, 15 Arabidopsis orthologs of 23 eukaryotic peroxin genes have been identified, but a function has been determined for only 4 of these 15 orthologs. Public access to this information will be available at (http://lsweb.la.asu.edu/rtreleaseq). The function(s) of these PMPs will be determined experimentally through a multi-pronged approach, i.e., elucidation of their subcellular localization, intracellular sorting pathways, and molecular sorting signals in suspension cells from wild type and mutant plants, and developmentally through interactions of RNAs with increasingly available ESTs on microarrays. Also, phenotypic and functional complementation results obtained with available T-DNA knockouts will be examined. Experimental results will be presented by students and postdoctoral persons attending local and national meetings, and will be published in refereed journal articles. The research is expected to elucidate the function of at least 10 genes related to the biogenesis and functioning of peroxisomes in Arabidopsis; this is consistent with the Objectives of the 2010 Project. Since peroxisomal mutations are lethal in humans, and peroxisomes are essential for seedling establishment and photo-autotrophic growth of oilseed and other crop plants, the knowledge obtained for functions of Arabidopsis peroxisomal genes can and very likely will be applied to biotechnological improvements of agriculturally-important crop plants, and to possibly speed therapeutic resolution of peroxisomal biogenetic diseases in human infants.

PUBLICATIONS PRODUCED AS A RESULT OF THIS RESEARCH

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Flynn CR, M Heinze, U Schumann, C Gietl, RN Trelease.  "Compartmentation of the plant peroxin, AtPex10p, within domain(s) of ER.,"  Plant Science,  v.168,  2005,  p. 635.

Hunt, J and RN Trelease.  "Sorting pathway and molecular targeting signal for the Arabidopsis peroxin 3,"  Biochem Biophys Res Comm,  v.314,  2004,  p. 586.

Karnik SK and RN Trelease.  "Arabidopsis Peroxin 16 trafficks through the ER and an intermediate compartment to pre-existing peroxisomes via overlapping molecular targeting signals.,"  Jour Experimental Botany,  v.58,  2007,  p. 1677.

Karnik, SK and RN Trelease.  "Arabidopsis peroxin 16 coexists at steady state in peroxisomes and endoplasmic reticulum. Plant Physiol 138:1967-1983.,"  Plant Physiol,  v.138,  2005,  p. 1967.

Leivar, L., VM Gonzalez, S Castel, RN Trelease, A Boronat, N Campos, A Ferrer, X Fernandez-Busquets.  "Subcellular localization of Arabidopsis 3-hydroxy-3-methylgutaryl-Coenzyme A reductase.,"  Plant Physiology,  v.137,  2005,  p. 57.

Lingard MJ and RN Trelease.  "Five Arabidopsis peroxin 11 homologs individually promote peroxisome elongation, division without elongation, or aggregation.,"  Jour Cell Sci,  v.119,  2006,  p. 1961.

Lisenbee CS, M Heinze, RN Trelease.  "Peroxisomal ascorbate peroxidase resides within a subdomain of rough endoplasmic reticulum in wildtype Arabidopsis cells,"  Plant Physiology,  v.132,  2003,  p. 870.

Lisenbee CS, MJ Lingard, RN Trelease.  "Arabidopsis peroxisomes possess functionally redundant membrane and matrix isoforms of monodehydroascorbate reductase.,"  The Plant Journal,  v.43,  2005,  p. 900.

Lisenbee CS, SK Karnik, RN Trelease.  "Overexpression and mislocalization of a tail-anchored GFP redefines the identity of peroxisomal ER,"  Traffic,  v.4,  2003,  p. 491.

Mullen RT and RN Trelease.  "The ER-peroxisome connection in plants: development of the "ER semi-autonomous peroxisome maturation and replication" model for plant peroxisome biogenesis.,"  Biochim Biophys Acta - Molecular Cell Research.,  v.1763,  2006,  p. 1655.


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