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

This Article Full Text Full Text (PDF) An addition or correction has been published Alert me when this article is cited 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 Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Bito, A. Articles by Breitenbach, M. Search for Related Content PubMed PubMed Citation Articles by Bito, A. Articles by Breitenbach, M. Social Bookmarking                      What's this?

Volume 272, Number 34, Issue of August 22, 1997 pp. 21509-21519
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Identification and Phenotypic Analysis of Two Glyoxalase II Encoding Genes from Saccharomyces cerevisiae, GLO2 and GLO4, and Intracellular Localization of the Corresponding Proteins

(Received for publication, April 9, 1997)

From the Institute for Genetics and General Biology, University of Salzburg, A-5020 Salzburg, Austria

We have isolated and characterized two genes coding for the glyoxalase II enzyme from Saccharomyces cerevisiae. The coding region of the GLO2 gene corresponds to a protein with 274 amino acids and a molecular mass of 31,306 daltons. The open reading frame of the GLO4 gene could be translated into a protein with 285 amino acids and a molecular mass of 32,325 daltons. The amino acid sequences of the deduced proteins are 59.1% identical and show high similarities to the sequence of the human glyoxalase II. When grown on either glucose or glycerol as a carbon source, a glo2 glo4 double deletion strain contains no glyoxalase II activity at all and shows no obvious phenotype during vegetative growth. However, this strain showed a similar high sensitivity against exogenous methylglyoxal as compared with a glyoxalase I-deficient strain. Whereas the GLO2 gene is expressed on both glucose and glycerol, the GLO4 gene is only active on glycerol. The active Glo2p protein is localized in the cytoplasm and the active Glo4p in the mitochondrial matrix. Heterologous expression of the full-length GLO2 coding region in Escherichia coli resulted in an active protein. However, to get an active Glo4p protein in E. coli, the putative mitochondrial transit peptide at the N-terminal end had to be removed by shortening the 5 end of the GLO4 open reading frame.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				M. Deponte, N. Sturm, S. Mittler, M. Harner, H. Mack, and K. Becker Allosteric Coupling of Two Different Functional Active Sites in Monomeric Plasmodium falciparum Glyoxalase I J. Biol. Chem., September 28, 2007; 282(39): 28419 - 28430. [Abstract] [Full Text] [PDF]

				Y. Takatsume, S. Izawa, and Y. Inoue Methylglyoxal as a Signal Initiator for Activation of the Stress-activated Protein Kinase Cascade in the Fission Yeast Schizosaccharomyces pombe J. Biol. Chem., April 7, 2006; 281(14): 9086 - 9092. [Abstract] [Full Text] [PDF]

				G. P. K. Marasinghe, I. M. Sander, B. Bennett, G. Periyannan, K.-W. Yang, C. A. Makaroff, and M. W. Crowder Structural Studies on a Mitochondrial Glyoxalase II J. Biol. Chem., December 9, 2005; 280(49): 40668 - 40675. [Abstract] [Full Text] [PDF]

				A. Zuin, A. P. Vivancos, M. Sanso, Y. Takatsume, J. Ayte, Y. Inoue, and E. Hidalgo The Glycolytic Metabolite Methylglyoxal Activates Pap1 and Sty1 Stress Responses in Schizosaccharomyces pombe J. Biol. Chem., November 4, 2005; 280(44): 36708 - 36713. [Abstract] [Full Text] [PDF]

				K. Maeta, S. Izawa, and Y. Inoue Methylglyoxal, a Metabolite Derived from Glycolysis, Functions as a Signal Initiator of the High Osmolarity Glycerol-Mitogen-activated Protein Kinase Cascade and Calcineurin/Crz1-mediated Pathway in Saccharomyces cerevisiae J. Biol. Chem., January 7, 2005; 280(1): 253 - 260. [Abstract] [Full Text] [PDF]

				H.-Y. Lee, Y. Xu, Y. Huang, A. H. Ahn, G. W.J. Auburger, M. Pandolfo, H. Kwiecinski, D. A. Grimes, A. E. Lang, J. E. Nielsen, et al. The gene for paroxysmal non-kinesigenic dyskinesia encodes an enzyme in a stress response pathway Hum. Mol. Genet., December 15, 2004; 13(24): 3161 - 3170. [Abstract] [Full Text] [PDF]

				K. Maeta, S. Izawa, S. Okazaki, S. Kuge, and Y. Inoue Activity of the Yap1 Transcription Factor in Saccharomyces cerevisiae Is Modulated by Methylglyoxal, a Metabolite Derived from Glycolysis Mol. Cell. Biol., October 1, 2004; 24(19): 8753 - 8764. [Abstract] [Full Text] [PDF]

				P. A. Cordell, T. S. Futers, P. J. Grant, and R. J. Pease The Human Hydroxyacylglutathione Hydrolase (HAGH) Gene Encodes Both Cytosolic and Mitochondrial Forms of Glyoxalase II J. Biol. Chem., July 2, 2004; 279(27): 28653 - 28661. [Abstract] [Full Text] [PDF]

				S. Zou, S. Meadows, L. Sharp, L. Y. Jan, and Y. N. Jan Genome-wide study of aging and oxidative stress response in Drosophilamelanogaster PNAS, November 22, 2000; (2000) 260496697. [Abstract] [Full Text]

				G. KIZIL, K. WILKS, D. WELLS, and D.A. A. ALA'ALDEEN Detection and characterisation of the genes encoding glyoxalase I and II from Neisseria meningitidis J. Med. Microbiol., July 1, 2000; 49(7): 669 - 673. [Abstract] [Full Text] [PDF]

				S. Zou, S. Meadows, L. Sharp, L. Y. Jan, and Y. N. Jan Genome-wide study of aging and oxidative stress response in Drosophilamelanogaster PNAS, December 5, 2000; 97(25): 13726 - 13731. [Abstract] [Full Text] [PDF]