PHOSPHORYLATION OF SYNTHETIC ACIDIC PEPTIDES BY CASEIN KINASE-II - EVIDENCE FOR COMPETITION WITH PHOSPHORYLATION OF PROTEINS INVOLVED IN TRANSCRIPTION

被引：16

作者：

ANGIOLILLO, A ^{[1
]}

BRAMUCCI, M ^{[1
]}

MARSILI, V ^{[1
]}

PANARA, F ^{[1
]}

MIANO, A ^{[1
]}

AMICI, D ^{[1
]}

GIANFRANCESCHI, GL ^{[1
]}

机构：

[1] UNIV CAMERINO,DEPT MCA BIOL,I-62032 CAMERINO,ITALY

来源：

MOLECULAR AND CELLULAR BIOCHEMISTRY | 1993年 / 125卷 / 01期

关键词：

CASEIN KINASE-II; CKII; PHOSPHOPEPTIDES; NUCLEAR PROTEINS; TRANSCRIPTION;

D O I：

10.1007/BF00926836

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Phosphorylation of several synthetic acidic peptides by biochemically isolated casein kinase II (CKII) and by cellular and nuclear extracts containing CKII-like activity has been investigated. Especially the synthetic peptide pyroGlu-Asp-Asp-Ser-Asp-Glu-Glu-Asn comprising the carboxy-terminal acidic hepta-peptide of the largest subunit of RNA polymerase II was found to serve as an excellent substrate for purified CKII. Moreover, this peptide reduces the rate of 'in vitro' ATP-dependent stimulation of DNA transcription induced by the proteins in the extracts. Since the peptide itself is also significantly phosphorylated in such assays, it is supposed that it serves as a competitive substrate for the phosphorylation of proteins in the extracts whose phosphorylation seems to be a prerequisite for their activity in the transcription process. This points to the involvement of CKII and substrate(s) of CKII in the process of transcription.

引用

页码：65 / 72

页数：8

共 25 条

[1] LOW-MOLECULAR-WEIGHT PEPTIDE INHIBITS RNA-SYNTHESIS IN HUMAN LEUKEMIC AND PHYTOHEMAGGLUTININ-STIMULATED LEUKOCYTES AND GLOBIN MESSENGER-RNA TRANSCRIPTION IN DIFFERENTIATING FRIEND CELLS - (CALF THYMUS COMPLEMENTARY[H-3] DNA HYBRIDIZATION CELL DIFFERENTIATION) [J].