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Titolo:
A mutation within the catalytic domain of COT 1 kinase confers changes in the presence of two COT 1 isoforms and in Ser/Thr protein kinase and phosphatase activities in Neurospora crassa
Autore:
Gorovits, R; Propheta, O; Kolot, M; Dombradi, V; Yarden, O;
Indirizzi:
Hebrew Univ Jerusalem, Fac Agr Food & Environm Qual Sci, Dept Plant Pathol& Microbiol, IL-76100 Rehovot, Israel Hebrew Univ Jerusalem Rehovot Israel IL-76100 , IL-76100 Rehovot, Israel Hebrew Univ Jerusalem, Fac Agr Food & Environm Qual Sci, Otto Warburg Ctr Agr Biotechnol, IL-76100 Rehovot, Israel Hebrew Univ Jerusalem Rehovot Israel IL-76100 , IL-76100 Rehovot, Israel Tel Aviv Univ, Dept Biochem, IL-69978 Tel Aviv, Israel Tel Aviv Univ Tel Aviv Israel IL-69978 iochem, IL-69978 Tel Aviv, Israel Debrecen Univ Med, Sch Med, Dept Med Chem, H-4012 Debrecen, Hungary Debrecen Univ Med Debrecen Hungary H-4012 Chem, H-4012 Debrecen, Hungary
Titolo Testata:
FUNGAL GENETICS AND BIOLOGY
fascicolo: 2-3, volume: 27, anno: 1999,
pagine: 264 - 274
SICI:
1087-1845(199907/08)27:2-3<264:AMWTCD>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
MYOTONIC-DYSTROPHY KINASE; NUCLEAR-DISTRIBUTION; CYTOPLASMIC DYNEIN; MYOSIN PHOSPHATASE; HYPHAL GROWTH; RHO-KINASE; CELL-SHAPE; GENE; ENCODES; SUBUNIT;
Keywords:
calcineurin; COT1 kinase; dynactin; fungal growth and development; Neurospora crassa;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
36
Recensione:
Indirizzi per estratti:
Indirizzo: Dombradi, V Hebrew Univ Jerusalem, Fac Agr Food & Environm Qual Sci, Dept Plant Pathol& Microbiol, IL-76100 Rehovot, Israel Hebrew Univ Jerusalem Rehovot Israel IL-76100 ehovot, Israel
Citazione:
R. Gorovits et al., "A mutation within the catalytic domain of COT 1 kinase confers changes in the presence of two COT 1 isoforms and in Ser/Thr protein kinase and phosphatase activities in Neurospora crassa", FUNGAL G B, 27(2-3), 1999, pp. 264-274

Abstract

Neurospora crassa grows by forming spreading colonies. cot-1 belongs to a class of N. crassa colonial temperature-sensitive (cot) mutants and encodesa Ser/Thr protein kinase. We have mapped the cot-1 mutation to a single base change resulting in a His to Arg substitution at amino acid 351, which resides within the catalytic domain, Antibodies raised against COT1 detectedand immunoprecipitated a predominant 73-kDa polypeptide in N. crassa extracts, whose abundance was constant under all growth conditions tested. An additional, lower MW COT1 isoform (67-kDa) present in the wild-type was not detected in cot-1 grown at the restrictive temperature. Similarly, this isoform was not detected in cot-3 or cot-5 strains, when grown at restrictive temperatures. Reduced levels of Ser/Thr kinase activity and an increase in type 1 and type 2B phosphatase (calcineurin) activities were measured in a cot-1 background. Apparent changes in the phosphorylation state of the p150(Glued) subunit of the dynactin cytoskeletal motor component (encoded by ro-3, a suppressor of cot-1) and evidence of in vitro physical interactions between COT1 and calcineurin indicate a functional linkage among COT1 kinase,type 2B phosphatase, and dynactin. (C) 1999 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/01/21 alle ore 09:58:53