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Titolo:
EVIDENCE THAT HETR PROTEIN IS AN UNUSUAL SERINE-TYPE PROTEASE
Autore:
ZHOU RB; WEI XC; JIANG N; LI HG; DONG YQ; HSI KL; ZHAO JD;
Indirizzi:
BEIJING UNIV,COLL LIFE SCI BEIJING 100871 PEOPLES R CHINA BEIJING UNIV,COLL LIFE SCI BEIJING 100871 PEOPLES R CHINA APPL BIOSYST INC FOSTER CITY CA 94404
Titolo Testata:
Proceedings of the National Academy of Sciences of the United Statesof America
fascicolo: 9, volume: 95, anno: 1998,
pagine: 4959 - 4963
SICI:
0027-8424(1998)95:9<4959:ETHPIA>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
HETEROCYST DIFFERENTIATION; POLYVINYLIDENE DIFLUORIDE; PROTEOLYSIS; ANABAENA; GENE; SITE; EXPRESSION; MEMBRANES; SEQUENCE;
Keywords:
CYANOBACTERIA; ANABAENA PCC7120; HETEROCYST DIFFERENTIATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
28
Recensione:
Indirizzi per estratti:
Citazione:
R.B. Zhou et al., "EVIDENCE THAT HETR PROTEIN IS AN UNUSUAL SERINE-TYPE PROTEASE", Proceedings of the National Academy of Sciences of the United Statesof America, 95(9), 1998, pp. 4959-4963

Abstract

The hetR gene plays a very important role in cell differentiation of heterocystous cyanobacteria, To understand the mechanism of the hetR gene product in regulation of heterocyst differentiation, the recombinant HetR protein (rHetR) was overproduced in Escherichia coli, PurifiedrHetR was unstable and degraded easily in solution, Phenylmethanesulfonyl fluoride, a serine-type protease inhibitor, prevented the degradation and was shown to modify covalently rHetR, Dansyl fluoride (DnsF),another serine-type protease inhibitor, also covalently modifies rHetR as shown by electrophoresis and electroblotting of the labeled rHetRand by MS. The labeling of rHetR with phenylmethanesulfonyl fluoride and DnsF was at the same site of rHetR and required Ca2+. S179N-rHetR,a mutant protein from strain 216 of Anabaena PCC 7120, which cannot differentiate heterocysts because of the mutation, was also overproduced and characterized. Although S170N-rHetR still can be labeled with DnsF, no proteolysis was observed, suggesting that Ser179 is involved inproteolytic activity. DnsF-labeled rHetR was digested with trypsin, and the labeled peptide was isolated and sequenced, The labeled peptidematches a sequence from HetR, These results show that HetR is a protease.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/03/20 alle ore 13:34:00