Nonorganellar acyl carrier protein from oleaginous yeast is a homologue of ribosomal protein P2

Sumana Raychaudhuri, Ram Rajasekharan

Research output: Contribution to journalArticle

Abstract

Acyl carrier protein (ACP) is responsible for carrying the growing fatty acid chain from one enzyme active site to the next during fatty acid biosynthesis. Here we report the identification, purification, immunocytochemical localization, and cloning of ACP from the oleaginous yeast, Rhodotorula glutinis. The soluble fraction of this organism can synthesize triacylglycerol and is able to accept the acyl group from acyl-ACP for the synthesis. The ACP, cloned from the system, showed a significant similarity with ribosomal protein P2. Expression and characterization of the recombinant protein showed that the ACP was acylated in vitro. The recombinant protein was post-translationally modified, since it was observed in [14C] β-alanine labeling and matrix-assisted laser desorption mass spectroscopic analysis. Site-directed mutants were generated to identify a serine residue responsible for phosphopantetheinylation and found that mutation of serine 59 to alanine abrogated the fatty acylation ability of the protein. These results demonstrate that a novel modification of ribosomal protein P2 allows it to act as an acyl carrier protein and participate in acylation reactions.

Original languageEnglish (US)
Pages (from-to)37648-37657
Number of pages10
JournalJournal of Biological Chemistry
Volume278
Issue number39
DOIs
Publication statusPublished - Sep 26 2003
Externally publishedYes

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ASJC Scopus subject areas

  • Biochemistry

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