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Titolo:
Specific DNA binding and transactivation potential of recombinant, purified Stat5
Autore:
Beisenherz-Huss, C; Mundt, M; Herrala, A; Vihko, P; Schubert, A; Groner, B;
Indirizzi:
Inst Biomed Res, George Speyer Haus, D-60596 Frankfurt, Germany Inst Biomed Res Frankfurt Germany D-60596 us, D-60596 Frankfurt, Germany Univ Freiburg, Inst Anat, D-79104 Freiburg, Germany Univ Freiburg Freiburg Germany D-79104 t Anat, D-79104 Freiburg, Germany Univ Oulu, WHO Collaborating Ctr Res Reprod Hlth, Bioctr Oulu, FIN-90014 Oulu, Finland Univ Oulu Oulu Finland FIN-90014 h, Bioctr Oulu, FIN-90014 Oulu, Finland
Titolo Testata:
MOLECULAR AND CELLULAR ENDOCRINOLOGY
fascicolo: 1-2, volume: 183, anno: 2001,
pagine: 101 - 112
SICI:
0303-7207(20011025)183:1-2<101:SDBATP>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-TYROSINE KINASES; BETA-CASEIN GENE; SERINE PHOSPHORYLATION; MAMMARY-GLAND; TRANSCRIPTION FACTOR; MAXIMAL ACTIVATION; JAK-STAT5 PATHWAY; NUCLEAR FACTOR; PROLACTIN; REQUIRES;
Keywords:
recombinant Stat5; phosphorylation; phosphatase treatment; transactivation;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
36
Recensione:
Indirizzi per estratti:
Indirizzo: Groner, B Inst Biomed Res, George Speyer Haus, Paul Ehrlich Str 42, D-60596 Frankfurt, Germany Inst Biomed Res Paul Ehrlich Str 42 Frankfurt GermanyD-60596 y
Citazione:
C. Beisenherz-Huss et al., "Specific DNA binding and transactivation potential of recombinant, purified Stat5", MOL C ENDOC, 183(1-2), 2001, pp. 101-112

Abstract

The signal transducers and activators of transcriptions (Stats) are central mediators of cytokine responses especially in hematopoietic cells. The detailed molecular mechanisms of Stat activation, particularly the role of post-translational modifications and co-operation with cellular transcriptionfactors are subject to intense investigation. The phosphorylation of a tyrosine residue in the carboxyl terminal domain is a common characteristic for the biologically active state of all known Stats. We studied the biological potential of purified recombinant murine Stat5a and Stat5b. These proteins were expressed in Sf9 insect cells upon infection with Stat5 encoding baculoviruses. We also obtained the tyrosine phosphorylated, activated forms of the Stat5 proteins by expressing the tyrosine kinase Janus kinase2 (Jak)in the same cells through co-infection with a kinase encoding virus. Afterpurification, only the tyrosine phosphorylated form was able to bind specifically in vitro to the Stat5 DNA response element. This activated form of Stat5 is also able to support specific cell free in vitro transcription of a gene with a Stat5 response element in its promoter region. The recombinant purified Stat5 proteins were treated with the tyrosine specific protein phosphatase or with potato acidic phosphatase, which removes phosphate groups from serine and tyrosine residues. Phosphatase treatment resulted in the loss of specific DNA binding ability. This property could be restored by anin vitro reaction with recombinant, purified EGF or PDGF receptor kinases. Tyrosine rephosphorylation in vitro also restored the transactivation potential of Stat5. This modification is, therefore. a sufficient prerequisite for transcriptional induction by Stat5. (C) 2001 Elsevier Science Ireland Ltd. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 15/08/20 alle ore 19:18:35