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Titolo:
The yeast Chs4 protein stimulates the trypsin-sensitive activity of chitinsynthase 3 through an apparent protein-protein interaction
Autore:
Ono, N; Yabe, T; Sudoh, M; Nakajima, T; Yamada-Okabe, T; Arisawa, M; Yamada-Okabe, H;
Indirizzi:
Yokohama City Univ, Sch Med, Dept Hyg, Kanazawa Ku, Yokohama, Kanagawa 2360004, Japan Yokohama City Univ Yokohama Kanagawa Japan 2360004 anagawa 2360004, Japan Tohoku Univ, Grad Sch Agr Sci, Div Life Sci, Aoba Ku, Sendai, Miyagi 9818555, Japan Tohoku Univ Sendai Miyagi Japan 9818555 Ku, Sendai, Miyagi 9818555, Japan Nippon Roche Res Ctr, Dept Mycol, Kamakura, Kanagawa 2478530, Japan NipponRoche Res Ctr Kamakura Kanagawa Japan 2478530 agawa 2478530, Japan
Titolo Testata:
MICROBIOLOGY-UK
, volume: 146, anno: 2000,
parte:, 2
pagine: 385 - 391
SICI:
1350-0872(200002)146:<385:TYCPST>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
POLARIZED GROWTH SITES; SACCHAROMYCES-CEREVISIAE; KLUYVEROMYCES-LACTIS; S-CEREVISIAE; KILLER TOXIN; CELL-WALL; GENE; BIOSYNTHESIS; TRAFFICKING; RESISTANCE;
Keywords:
yeast; chitin synthase 3; overexpression; protein-protein interaction;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
31
Recensione:
Indirizzi per estratti:
Indirizzo: Yamada-Okabe, H Yokohama City Univ, Sch Med, Dept Hyg, Kanazawa Ku, 3-9 Fukuura, Yokohama,Kanagawa 2360004, Japan Yokohama City Univ 3-9 Fukuura Yokohama Kanagawa Japan 2360004
Citazione:
N. Ono et al., "The yeast Chs4 protein stimulates the trypsin-sensitive activity of chitinsynthase 3 through an apparent protein-protein interaction", MICROBIO-UK, 146, 2000, pp. 385-391

Abstract

Inducible overexpression of the CHS4 gene under the control of the GAL1 promoter increased Chs3p (chitin synthase 3) activity in Saccharomyces promoter increased Chs3p (chitin synthase 3) activity in Saccharomyces cerevisiaeseveral fold, Approximately half of the Chs3p activity in the membranes ofcells overexpressing Chs4p was extracted using CHAPS and cholesteryl hemisuccinate. The detergent-extractable Chs3p activity appeared to be non-zymogenic because incubation with trypsin decreased enzyme activity in both the presence and absence of the substrate, UDP-N-acetylglucosamine, Western blotting confirmed that Chs3p was extracted from membranes by CHAPS and cholesteryl hemisuccinate and revealed that Chs4p was also solubilized using these detergents, Yeast two-hybrid analysis with truncated Chs4p demonstrated that the region of Chs4p between amino acids 269 and 563 is indispensable not only for eliciting the non-zymogenic activity Of Chs3p but also for binding of Chs4p to Chs3p, Neither the EF-hand motif nor a possible prenylation site in Chs4p was required for these activities, Thus, it was demonstrated that stimulation of non-zymogenic Chs3p activity by Chs4p requires the amino acid region from 269 to 563 of Chs4p, and it seems that Chs4p activates Chs3p through protein-protein interaction.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 09/07/20 alle ore 20:48:45