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Titolo:
THE C-TERMINAL HALF OF THE ANTI-SIGMA FACTOR, FLGM, BECOMES STRUCTURED WHEN BOUND TO ITS TARGET, SIGMA(28)
Autore:
DAUGHDRILL GW; CHADSEY MS; KARLINSEY JE; HUGHES KT; DAHLQUIST FW;
Indirizzi:
UNIV OREGON,INST MOL BIOL EUGENE OR 97403 UNIV OREGON,INST MOL BIOL EUGENE OR 97403 UNIV WASHINGTON,DEPT MICROBIOL SEATTLE WA 98195
Titolo Testata:
Nature structural biology
fascicolo: 4, volume: 4, anno: 1997,
pagine: 285 - 291
SICI:
1072-8368(1997)4:4<285:TCHOTA>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
SALMONELLA-TYPHIMURIUM; FLAGELLAR FILAMENT; IMPROVED SENSITIVITY; HETERONUCLEAR NMR; SPECTROSCOPY; PROTEINS; EXPORT; MEMBRANE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
26
Recensione:
Indirizzi per estratti:
Citazione:
G.W. Daughdrill et al., "THE C-TERMINAL HALF OF THE ANTI-SIGMA FACTOR, FLGM, BECOMES STRUCTURED WHEN BOUND TO ITS TARGET, SIGMA(28)", Nature structural biology, 4(4), 1997, pp. 285-291

Abstract

The interaction between the flagellum specific sigma factor, sigma(28), and its inhibitor, FlgM, was examined using multidimensional heteronuclear NMR. Here we observe that free FlgM is mostly unfolded, but about 50% of the residues become structured when bound to sigma(28). Ouranalysis suggests that the sigma(28) binding domain of FlgM is contained within the last 57 amino acids of the protein while the first 40 amino acids are unstructured in both the free and bound states. Geneticanalysis of flgM mutants that fail to inhibit sigma(28) activity reveal amino acid changes that are also isolated to the C-terminal 57 residues of FlgM. We postulate that the lack of structure in free and bound FlgM is important to its role as an exported protein.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 12/08/20 alle ore 20:53:42