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Titolo:
A novel putative transcription factor protein MYT2 that preferentially binds supercoiled DNA and induces DNA synthesis in quiescent cells
Autore:
Shao, W; Lee, AY; Gulnik, S; Gustchina, E; Liu, YL; Kung, HF; Erickson, JW;
Indirizzi:
NCI, Struct Biochem Program, SAIC Frederick, Frederick Canc Res & Dev Ctr,Frederick, MD 21702 USA NCI Frederick MD USA 21702 ick Canc Res & Dev Ctr,Frederick, MD 21702 USA NCI, Lab Biochem Physiol, Frederick, MD 21702 USA NCI Frederick MD USA 21702 , Lab Biochem Physiol, Frederick, MD 21702 USA Univ Hong Kong, Inst Mol Biol, Hong Kong, Hong Kong, Peoples R China Univ Hong Kong Hong Kong Hong Kong Peoples R China Kong, Peoples R China
Titolo Testata:
FEBS LETTERS
fascicolo: 3, volume: 473, anno: 2000,
pagine: 363 - 369
SICI:
0014-5793(20000519)473:3<363:ANPTFP>2.0.ZU;2-R
Fonte:
ISI
Lingua:
ENG
Soggetto:
REPLICATION INITIATOR PROTEIN; SEQUENCE SPECIFICITY; HUMAN FIBROBLASTS; SUPERHELICAL DNA; NUCLEAR-PROTEIN; IN-VITRO; PROMOTER; SITES; TRANSFORMATION; MICROINJECTION;
Keywords:
myelin transcription factor 2; DNA-binding protein; topoisomer-like pattern; DNA replicase; DNA synthesis; microinjection;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
34
Recensione:
Indirizzi per estratti:
Indirizzo: Shao, W Celera Genom, 45 W Gude Dr, Rockville, MD 20850 USA Celera Genom 45 W Gude Dr Rockville MD USA 20850 lle, MD 20850 USA
Citazione:
W. Shao et al., "A novel putative transcription factor protein MYT2 that preferentially binds supercoiled DNA and induces DNA synthesis in quiescent cells", FEBS LETTER, 473(3), 2000, pp. 363-369

Abstract

Myelin transcription factor 2 (MYT2), a putative transcription factor found in the human central nervous system, was cloned from an expression cDNA library from human T-cells, MYT2 shares weak similarity to bacterial type I topoisomerases and shares 63% sequence identity to a replicase from Leuconostoc mesenteroides. MYT2 preferentially binds supercoiled DNA (scDNA), Incubation of MYT2 and scDNA at or above equal molar ratios generated topoisomer-like patterns that were abolished by deproteination. Thus, MYT2 appears to relax scDNA via a non-enzymatic mechanism. The banding pattern of MYT2-scDNA complexes was shown to be quantisized, saturable and sequence-independent. Microinjection of MYT2 mRNA induced G(0) growth-arrested NIH 3T3 cells to enter the S phase of the cell cycle, (C) 2000 Federation of European Biochemical Societies.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 22/01/20 alle ore 18:25:31