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

J. Biol. Chem., Vol. 278, Issue 3, 1480-1486, January 17, 2003

This Article Full Text Full Text (PDF) All Versions of this Article: 278/3/1480    most recent M209395200v1 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 Williams, R. A. M. Articles by Coombs, G. H. Search for Related Content PubMed PubMed Citation Articles by Williams, R. A. M. Articles by Coombs, G. H. Social Bookmarking                      What's this?

3-Mercaptopyruvate Sulfurtransferase of Leishmania Contains an Unusual C-terminal Extension and Is Involved in Thioredoxin and Antioxidant Metabolism^*

Roderick A. M. Williams^§, Sharon M. Kelly^¶, Jeremy C. Mottram^**, and Graham H. Coombs

From the Divisions of  Infection and Immunity and ^¶ Biochemistry and Molecular Biology, Institute of Biomedical and Life Sciences, University of Glasgow, Glasgow G12 8QQ and the  Wellcome Centre for Molecular Parasitology, University of Glasgow, Anderson College, Glasgow G11 6NU, Scotland, United Kingdom

Cytosolic 3-mercaptopyruvate sulfurtransferases (EC 2.8.1.2) of Leishmania major and Leishmania mexicana have been cloned, expressed as active enzymes in Escherichia coli, and characterized. The leishmanial single-copy genes predict a sulfurtransferase that is structurally peculiar in possessing a C-terminal domain of some 70 amino acids. Homologous genes of Trypanosoma cruzi and Trypanosoma brucei encode enzymes with a similar C-terminal domain, suggesting that this feature, not known in any other sulfurtransferase, is a characteristic of trypanosomatid parasites. Short truncations of the C-terminal domain resulted in misfolded inactive proteins, demonstrating that the domain plays some key role in facilitating correct folding of the enzymes. The leishmanial recombinant enzymes exhibited high activity toward 3-mercaptopyruvate and catalyzed the transfer of sulfane sulfur to cyanide to form thiocyanate. They also used thiosulfate as a substrate and reduced thioredoxin as the accepting nucleophile, the latter being oxidized. The enzymes were expressed in all life cycle stages, and the expression level was increased under peroxide or hypo-sulfur stress. The results are consistent with the enzymes having an involvement in the synthesis of sulfur amino acids per se or iron-sulfur centers of proteins and the parasite's management of oxidative stress.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AJ313201 and AJ313202.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				N. Nagahara, T. Yoshii, Y. Abe, and T. Matsumura Thioredoxin-dependent Enzymatic Activation of Mercaptopyruvate Sulfurtransferase: AN INTERSUBUNIT DISULFIDE BOND SERVES AS A REDOX SWITCH FOR ACTIVATION J. Biol. Chem., January 19, 2007; 282(3): 1561 - 1569. [Abstract] [Full Text] [PDF]

				G. D. Westrop, G. Goodall, J. C. Mottram, and G. H. Coombs Cysteine Biosynthesis in Trichomonas vaginalis Involves Cysteine Synthase Utilizing O-Phosphoserine J. Biol. Chem., September 1, 2006; 281(35): 25062 - 25075. [Abstract] [Full Text] [PDF]

				R. Zufferey and C. B. Mamoun Leishmania major Expresses a Single Dihydroxyacetone Phosphate Acyltransferase Localized in the Glycosome, Important for Rapid Growth and Survival at High Cell Density and Essential for Virulence J. Biol. Chem., March 24, 2006; 281(12): 7952 - 7959. [Abstract] [Full Text] [PDF]

				N. Nagahara and A. Katayama Post-translational Regulation of Mercaptopyruvate Sulfurtransferase via a Low Redox Potential Cysteine-sulfenate in the Maintenance of Redox Homeostasis J. Biol. Chem., October 14, 2005; 280(41): 34569 - 34576. [Abstract] [Full Text] [PDF]

				M. S. Alphey, R. A. M. Williams, J. C. Mottram, G. H. Coombs, and W. N. Hunter The Crystal Structure of Leishmania major 3-Mercaptopyruvate Sulfurtransferase: A THREE-DOMAIN ARCHITECTURE WITH A SERINE PROTEASE-LIKE TRIAD AT THE ACTIVE SITE J. Biol. Chem., November 28, 2003; 278(48): 48219 - 48227. [Abstract] [Full Text] [PDF]