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001-es BibID:	BIBFORM027915
Első szerző:	Gorovits, Rena
Cím:	A mutation within the catalytic domain of COT1 kinase confers changes in the presence of two COT1 isoforms and in Ser/Thr protein kinase and phosphatase activities in Neurospora crassa / Rena Gorovits, Oshrat Propheta, Mikhail Kolot, Viktor Dombradi, Oded Yarden
Dátum:	1999
Megjegyzések:	Neurospora crassa grows by forming spreading colonies. cot-1 belongs to a class of N. crassa colonial temperature-sensitive (cot) mutants and encodes a 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 detected and 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.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban COT1 Ser/Thr protein kinase Neurospora crassa
Megjelenés:	Fungal Genetics and Biology. - 27 : 2-3 (1999), p. 264-274. -
További szerzők:	Propheta, Oshrat Kolot, Mikhail Yarden, Oded Dombrádi Viktor (1953-) (biokémikus)
Internet cím:	Intézményi repozitóriumban (DEA) tárolt változat DOI
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