Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
METALLOADSORPTION BY ESCHERICHIA-COLI-CELLS DISPLAYING YEAST AND MAMMALIAN METALLOTHIONEINS ANCHORED TO THE OUTER-MEMBRANE PROTEIN LAMB
Autore:
SOUSA C; KOTRBA P; RUML T; CEBOLLA A; DELORENZO V;
Indirizzi:
CSIC,CTR NACL BIOTECNOL,CAMPUS CANTOBLANCO E-28049 MADRID SPAIN CSIC,CTR NACL BIOTECNOL E-28049 MADRID SPAIN INST CHEM TECHNOL,DEPT BIOCHEM & MICROBIOL CR-16628 PRAGUE CZECH REPUBLIC
Titolo Testata:
Journal of bacteriology
fascicolo: 9, volume: 180, anno: 1998,
pagine: 2280 - 2284
SICI:
0021-9193(1998)180:9<2280:MBEDYA>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
DISULFIDE BOND FORMATION; PROKARYOTIC METALLOTHIONEIN; PSEUDOMONAS-PUTIDA; HEAVY-METALS; EXPRESSION; MECHANISMS; GENE; BIOTECHNOLOGY; RESISTANCE; INSERTION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
45
Recensione:
Indirizzi per estratti:
Citazione:
C. Sousa et al., "METALLOADSORPTION BY ESCHERICHIA-COLI-CELLS DISPLAYING YEAST AND MAMMALIAN METALLOTHIONEINS ANCHORED TO THE OUTER-MEMBRANE PROTEIN LAMB", Journal of bacteriology, 180(9), 1998, pp. 2280-2284

Abstract

Yeast (CUP1) and mammalian (HMT-1A) metallothioneins (MTs) have been efficiently expressed in Escherichia call as fusions to the outer membrane protein LamB. A 65-amino-acid sequence from the CUP1 protein of Saccharomyces cerevisiae (yeast [Y] MT) was genetically inserted in permissive site 153 of the LamB sequence, which faces the outer medium. Asecond LamB fusion at position 153 was created with 66 amino acids recruited from the form of human (H) MT that is predominant in the adipose tissue, HMT-1A. Both LamB(153)-YMT and LamB(153)-HMT hybrids were produced in vivo as full-length proteins, without any indication of instability or proteolytic degradation. Each of the two fusion proteins was functional as the port of entry of lambda phage variants, suggesting maintenance of the overall topology of the wild-type LamB. Expression of the hybrid proteins in vivo multiplied the natural ability. of E.coli cells to bind Cd2+ 15- to 20-fold, in good correlation with the number of metal-binding centers contributed by the MT moiety of the fusions.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 24/09/20 alle ore 04:49:08