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Titolo:
SYNTHESIS AND BIOCHEMICAL-CHARACTERIZATION OF AN ANALOG OF CHEY-PHOSPHATE, A SIGNAL-TRANSDUCTION PROTEIN IN BACTERIAL CHEMOTAXIS
Autore:
HALKIDES CJ; ZHU XY; PHILLION DP; MATSUMURA P; DAHLQUIST FW;
Indirizzi:
UNIV OREGON,INST MOL BIOL EUGENE OR 97403 UNIV OREGON,INST MOL BIOL EUGENE OR 97403 UNIV N CAROLINA,DEPT CHEM WILMINGTON NC 28403 UNIV ILLINOIS CHICAGO IL 60612 MONSANTO AGR PROD CO ST LOUIS MO 63198 UNIV ILLINOIS,DEPT MICROBIOL & IMMUNOL CHICAGO IL 60612
Titolo Testata:
Biochemistry (Easton)
fascicolo: 39, volume: 37, anno: 1998,
pagine: 13674 - 13680
SICI:
0006-2960(1998)37:39<13674:SABOAA>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
PHOSPHORYLATION-DEPENDENT BINDING; FLAGELLAR SWITCH; ESCHERICHIA-COLI; RESPONSE REGULATOR; SITE; SPECTROSCOPY; CONFORMATION; MUTATIONS; MOLECULE; MUTANTS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
38
Recensione:
Indirizzi per estratti:
Citazione:
C.J. Halkides et al., "SYNTHESIS AND BIOCHEMICAL-CHARACTERIZATION OF AN ANALOG OF CHEY-PHOSPHATE, A SIGNAL-TRANSDUCTION PROTEIN IN BACTERIAL CHEMOTAXIS", Biochemistry (Easton), 37(39), 1998, pp. 13674-13680

Abstract

CheY is a signal transduction protein of the bacterial chemotaxis system that acts as a molecular switch to alter the swimming behavior of the bacterium. When CheY becomes phosphorylated at Asp57, CheY-P-i interacts with flagellar motor proteins, including FliM, to increase the likelihood that the flagellar motor will change its sense of rotation,increasing the frequency of tumbling. The structure of CheY in its dephosphorylated (inactive) state has been intensively investigated. Theshort lifetime (similar to 20 s) of the aspartyl phosphate has precluded the complete structural determination of CheY-P-i. We have synthesized an analogue of CheY-P-i by alkylating an aspartate-to-cysteine mutant at position 57 of CheY to add a phosphonomethyl group at Cys57. This analogue, phosphono-CheY, is stable for months. Phosphono-CheY binds to two of the targets of CheY-P-i, FliM and CheZ, in a manner similar to that of CheY-P-i and much better than either unphosphorylated CheY or the unmodified form of D57C CheY, Phosphono-CheY also binds Mg(II) with a dissociation constant of similar to 6 mM at neutral pH and moderate salt level. These observations indicate that phosphono-CheY isa good biochemical analogue of CheY-P-i.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/07/20 alle ore 12:43:24