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Title: Identification of a novel CoA synthase isoform, which is primarily expressed in Brain

Journal Article · · Biochemical and Biophysical Research Communications
 [1];  [1];  [1];  [1];  [1];  [2]
  1. Department of Structure and Function of Nucleic Acids, Institute of Molecular Biology and Genetics, 150 Zabolotnogo St, Kyiv 03680 (Ukraine)
  2. Department of Structure and Function of Nucleic Acids, Institute of Molecular Biology and Genetics, 150 Zabolotnogo St, Kyiv 03680 (Ukraine) and Department of Biochemistry and Molecular Biology, Royal Free and University College Medical School, Gower Street, London WC1E 6BT (United Kingdom)

CoA and its derivatives Acetyl-CoA and Acyl-CoA are important players in cellular metabolism and signal transduction. CoA synthase is a bifunctional enzyme which mediates the final stages of CoA biosynthesis. In previous studies, we have reported molecular cloning, biochemical characterization, and subcellular localization of CoA synthase (CoASy). Here, we describe the existence of a novel CoA synthase isoform, which is the product of alternative splicing and possesses a 29aa extension at the N-terminus. We termed it CoASy {beta} and originally identified CoA synthase, CoASy {alpha}. The transcript specific for CoASy {beta} was identified by electronic screening and by RT-PCR analysis of various rat tissues. The existence of this novel isoform was further confirmed by immunoblot analysis with antibodies directed to the N-terminal peptide of CoASy {beta}. In contrast to CoASy {alpha}, which shows ubiquitous expression, CoASy {beta} is primarily expressed in Brain. Using confocal microscopy, we demonstrated that both isoforms are localized on mitochondria. The N-terminal extension does not affect the activity of CoA synthase, but possesses a proline-rich sequence which can bring the enzyme into complexes with signalling proteins containing SH3 or WW domains. The role of this novel isoform in CoA biosynthesis, especially in Brain, requires further elucidation.

OSTI ID:
20798851
Journal Information:
Biochemical and Biophysical Research Communications, Vol. 341, Issue 4; Other Information: DOI: 10.1016/j.bbrc.2006.01.051; PII: S0006-291X(06)00080-5; Copyright (c) 2006 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
Country of Publication:
United States
Language:
English