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Titolo:
Deletion of the cnxE gene encoding the gephyrin-like protein involved in the final stages of molybdenum cofactor biosynthesis in Aspergillus nidulans
Autore:
Millar, LJ; Heck, IS; Sloan, J; Kanan, GJM; Kinghorn, JR; Unkles, SE;
Indirizzi:
Monash Univ, Dept Microbiol, Clayton, Vic 3168, Australia Monash Univ Clayton Vic Australia 3168 biol, Clayton, Vic 3168, Australia Univ St Andrews, Sch Biol, St Andrews KY16 9TH, Fife, Scotland Univ St Andrews St Andrews Fife Scotland KY16 9TH Y16 9TH, Fife, Scotland Univ Tubingen, Inst Plant Biochem, D-72076 Tubingen, Germany Univ Tubingen Tubingen Germany D-72076 iochem, D-72076 Tubingen, Germany
Titolo Testata:
MOLECULAR GENETICS AND GENOMICS
fascicolo: 3, volume: 266, anno: 2001,
pagine: 445 - 453
SICI:
1617-4615(200111)266:3<445:DOTCGE>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
ESCHERICHIA-COLI; MOLYBDOPTERIN BIOSYNTHESIS; CRYSTAL-STRUCTURE; MUTANTS; CLONING; MOLYBDATE; MUTATIONS; PLANTS; OPERON; LOCUS;
Keywords:
fungi; molybdenum cofactor; cnxE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
47
Recensione:
Indirizzi per estratti:
Indirizzo: Unkles, SE Monash Univ, Dept Microbiol, Clayton, Vic 3168, Australia Monash Univ Clayton Vic Australia 3168 on, Vic 3168, Australia
Citazione:
L.J. Millar et al., "Deletion of the cnxE gene encoding the gephyrin-like protein involved in the final stages of molybdenum cofactor biosynthesis in Aspergillus nidulans", MOL GENET G, 266(3), 2001, pp. 445-453

Abstract

The Aspergillus nidulans cnxE gene, required for molybdenum cofactor biosynthesis, was isolated by functional complementation of an Escherichia coli mogA mutant strain. The deduced CnxE polypeptide consists of two domains which display similarity to the E. coli proteins MoeA and MogA, respectively,separated by a putative hinge region of around 58 amino acid residues which is notably histidine rich. A deletion mutant lacking the entire cnxE gene, including both MoeA-like and MogA-like domains, was identified, Compared to the wild type, a small increase in the intermediate precursor Z was observed in the deletion strain but was significant only under conditions in which the molybdoenzyme nitrate reductase was induced. Elevated levels of thepathway intermediate molybdopterin were found both under nitrate reductase-inducing and non-inducing conditions in the deletion mutant compared to the wild type. This increase is in contrast to previous results for cnxABC, cnxF, cnxG, and cnxH mutants, in which the levels of molybdopterin were substantially reduced, and therefore supports previously published classical genetic and biochemical studies that indicated that the CnxE protein is likely to be involved in the final stages of molybdenum cofactor biosynthesis. We have found no evidence during our chemical analysis for any involvement of this protein in the intermediate section of the molybdenum cofactor biosynthetic pathway (i.e. in the synthesis of molybdopterin from precursor Z), as has been suggested previously for E. coli MoeA. The 2.5-kb cnxE transcript is not abundant and appears to be expressed constitutively.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/03/20 alle ore 22:59:53