HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 277, Issue 12, 10435-10444, March 22, 2002

This Article Full Text Full Text (PDF) All Versions of this Article: 277/12/10435    most recent M111110200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Denis, L. Articles by Alban, C. Search for Related Content PubMed PubMed Citation Articles by Denis, L. Articles by Alban, C. Social Bookmarking                      What's this?

Molecular Characterization of a Second Copy of Holocarboxylase Synthetase Gene (hcs2) in Arabidopsis thaliana^*

Laurence Denis, Marie Grossemy, Roland Douce, and Claude Alban

From the Laboratoire mixte CNRS/INRA/Aventis (UMR 1932), Aventis cropscience, 14-20 rue Pierre Baizet, 69263 Lyon CEDEX 9, France

Holocarboxylase synthetase (HCS), catalyzing the covalent attachment of biotin, is ubiquitously represented in living organisms. Indeed, the biotinylation is a post-translational modification that allows the transformation of inactive biotin-dependent carboxylases, which are committed in fundamental metabolisms such as fatty acid synthesis, into their active holo form. Among other living organisms, plants present a peculiarly complex situation. In pea, HCS activity has been detected in three subcellular compartments and the systematic sequencing of the Arabidopsis genome revealed the occurrence of two hcs genes (hcs1 and hcs2). Hcs1 gene product had been previously characterized at molecular and biochemical levels. Here, by PCR amplification, we cloned an hcs2 cDNA from Arabidopsis thaliana (Ws ecotype) mRNA. We observed the occurrence of multiple cDNA forms which resulted from the alternative splicing of hcs2 mRNA. Furthermore, we evidenced a nucleotide polymorphism at the hcs2 gene within the Ws ecotype, which affected splicing of hcs2 mRNA. This contrasted sharply with the situation at hcs1 locus. However, this polymorphism had no apparent effect on total HCS activity in planta. Finally, hcs2 mRNAs were found 4-fold less abundant than hcs1 mRNA and the most abundant hcs2 mRNA spliced variant should code for a truncated protein. We discuss the possible role of such a multiplicity of putative HCS proteins in plants and discuss the involvement of each of hcs genes in the correct realization of biotinylation.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AF414935-AF414947.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				J. Puyaubert, L. Denis, and C. Alban Dual Targeting of Arabidopsis HOLOCARBOXYLASE SYNTHETASE1: A Small Upstream Open Reading Frame Regulates Translation Initiation and Protein Targeting Plant Physiology, February 1, 2008; 146(2): 478 - 491. [Abstract] [Full Text] [PDF]

				H. S. Kim, U. Hoja, J. Stolz, G. Sauer, and E. Schweizer Identification of the tRNA-binding Protein Arc1p as a Novel Target of in Vivo Biotinylation in Saccharomyces cerevisiae J. Biol. Chem., October 8, 2004; 279(41): 42445 - 42452. [Abstract] [Full Text] [PDF]