A lysine accumulation phenotype of Sclpk2Delta mutant yeast is rescued by Solanum tuberosum inositol phosphate multikinase

Caddick, Samuel E. K., Harrison, Christopher J., Stavridou, Ioanna, Johnson, Samuel and Brearley, Charles A. ORCID: https://orcid.org/0000-0001-6179-9109 (2007) A lysine accumulation phenotype of Sclpk2Delta mutant yeast is rescued by Solanum tuberosum inositol phosphate multikinase. Biochemical Journal, 403 (3). pp. 381-389. ISSN 0264-6021

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Abstract

Inositol phosphates and the enzymes that interconvert them are key regulators of diverse cellular processes including the transcriptional machinery of arginine synthesis [York (2006) Biochim. Biophys. Acta 1761, 552–559]. Despite considerable interest and debate surrounding the role of Saccharomyces cerevisiae inositol polyphosphate kinase (ScIPK2, ARG82, ARGRIII) and its inositol polyphosphate products in these processes, there is an absence of data describing how the transcripts of the arginine synthetic pathway, and the amino acid content of ScIpk2D, are altered under different nutrient regimes. We have cloned an IPMK (inositol phosphate multikinase) from Solanum tuberosum, StIPMK (GenBank® accession number EF362785), that despite considerable sequence divergence from ScIPK2, restores the arginine biosynthesis pathway transcripts ARG8, acetylornithine aminotransferase, and ARG3, ornithine carbamoyltransferase of ScIpk2D yeast to wild-type profiles. StIPMK also restores the amino acid profiles of mutant yeast to wild-type, and does so with ornithine or arginine as the sole nitrogen sources. Our data reveal a lysine accumulation phenotype in ScIpk2D yeast that is restored to a wild-type profile by expression of StIPMK, including restoration of the transcript profiles of lysine biosynthetic genes. The StIPMK protein shows only 18.6% identity with ScIPK2p which probably indicates that the rescue of transcript and diverse amino acid phenotypes is not mediated through a direct interaction of StIPMK with the ArgR–Mcm1 transcription factor complex that is a molecular partner of ScIPK2p.

Item Type:	Article
Faculty \ School:	Faculty of Science > School of Biological Sciences
UEA Research Groups:	Faculty of Science > Research Groups > Plant Sciences Faculty of Science > Research Groups > Molecular Microbiology
Depositing User:	EPrints Services
Date Deposited:	01 Oct 2010 13:38
Last Modified:	24 Sep 2024 09:38
URI:	https://ueaeprints.uea.ac.uk/id/eprint/1373
DOI:	10.1042/BJ20061772

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