Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
IDENTIFICATION OF THE STRUCTURAL AND FUNCTIONAL DOMAINS OF MUTY, AN ESCHERICHIA-COLI DNA MISMATCH REPAIR ENZYME
Autore:
MANUEL RC; CZERWINSKI EW; LLOYD RS;
Indirizzi:
UNIV TEXAS,MED BRANCH,SEALY CTR MOL SCI GALVESTON TX 77555 UNIV TEXAS,MED BRANCH,SEALY CTR MOL SCI GALVESTON TX 77555 UNIV TEXAS,MED BRANCH,SEALY CTR STRUCT BIOL GALVESTON TX 77555 UNIV TEXAS,MED BRANCH,DEPT HUMAN BIOL CHEM & GENET GALVESTON TX 77555
Titolo Testata:
The Journal of biological chemistry
fascicolo: 27, volume: 271, anno: 1996,
pagine: 16218 - 16226
SICI:
0021-9258(1996)271:27<16218:IOTSAF>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
G-A MISPAIRS; ENDONUCLEASE-III; FPG PROTEIN; ZINC-FINGER; GLYCOSYLASE; T4-ENDONUCLEASE-V; MECHANISM; DYNAMICS; TERMINUS; DUPLEX;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
40
Recensione:
Indirizzi per estratti:
Citazione:
R.C. Manuel et al., "IDENTIFICATION OF THE STRUCTURAL AND FUNCTIONAL DOMAINS OF MUTY, AN ESCHERICHIA-COLI DNA MISMATCH REPAIR ENZYME", The Journal of biological chemistry, 271(27), 1996, pp. 16218-16226

Abstract

The linear amino acid sequences of the Escherichia coli DNA repair proteins, MutY and endonuclease III, show significant homology, even though these enzymes recognize entirely different substrates, In this study, proteolysis and molecular modeling of MutY were used to elucidate its domain organization, Proteolysis by trypsin cleaved the enzyme into 26- and 13-kDa fragments, NH2-terminal sequencing showed that the pig domain begins at Gln(226), indicating that the COOH-terminal portionof MutY, absent in endonuclease III, is organized as a separate domain, The large p26 domain is almost equivalent to the size of endonuclease III. Binding activity of the p26 domain to a DNA substrate containing an A . G mismatch was comparable with that of the intact enzyme. Invitro studies show that the p26 domain retains adenine glycosylase and AP lyase activity on DNA containing undamaged adenine opposite guanine or 8-oxo-7,8-dihydro-2'-deoxyguanine. Although the activity was somewhat reduced, the above results show that the critical amino acid residues involved in substrate binding and catalysis are present in this domain. The structure predicted by molecular modeling indicates that the region of MutY (Met(1)-Trp(216)), which is homologous to endonuclease III exhibits a two domain structure, even though this portion is resistant to proteolysis by trypsin.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/09/20 alle ore 11:07:28