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Journal of Experimental Botany, Vol. 53, No. 379, pp. 2453-2454, December 1, 2002
© 2002 Oxford University Press

Isolation and expression analysis of the isopropylmalate synthase gene family of Arabidopsis thaliana

Received 29 July 2002; Accepted 21 August 2002

Damian J. Junk and George S. Mourad1,

Department of Biology, Indiana University-Purdue University Fort Wayne, 2101 E. Coliseum Blvd., Fort Wayne, IN 46805-1499, USA

1 To whom correspondence should be addressed. Fax: +1 219 481 6087. E-mail: mourad{at}ipfw.edu

Isopropylmalate synthase (IPMS) is the first enzyme in the leucine biosynthetic pathway. It is the branch point in the biosynthesis of leucine and the other branched-chain amino acids. IPMS is also regulated by negative feedback inhibition by the end-product leucine. There are four highly homologous loci within the Arabidopsis thaliana genome, which contain sequences that code for IPMS. Through library screening and RT-PCR the expression patterns of three of these loci namely IMS1, IMS2, and IMS3 have been isolated and then characterized. cDNAs of IMS2 and IMS3 lacking the 5' chloroplast leader sequence were able to complement a leucine auxotroph of E. coli.

Key words: Arabidopsis thaliana, functional complementation, isopropylmalate synthase (EC 4.1.3.12), leucine biosynthesis, ribonuclease protection assay.


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