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Titolo:
Functional analysis of the trypanosomal AAA protein TbVCP with trans-dominant ATP hydrolysis mutants
Autore:
Lamb, JR; Fu, V; Wirtz, E; Bangs, JD;
Indirizzi:
Univ Wisconsin, Sch Med, Dept Med Microbiol & Immunol, Madison, WI 53706 USA Univ Wisconsin Madison WI USA 53706 biol & Immunol, Madison, WI 53706 USA Rockefeller Univ, Mol Parasitol Lab, New York, NY 10021 USA Rockefeller Univ New York NY USA 10021 asitol Lab, New York, NY 10021 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 24, volume: 276, anno: 2001,
pagine: 21512 - 21520
SICI:
0021-9258(20010615)276:24<21512:FAOTTA>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
SENSITIVE FUSION PROTEIN; TRANSITIONAL ENDOPLASMIC-RETICULUM; VALOSIN-CONTAINING PROTEIN; MITOTIC GOLGI FRAGMENTS; MEMBRANE-FUSION; CELL-CYCLE; SACCHAROMYCES-CEREVISIAE; PEROXISOME BIOGENESIS; VESICULAR TRANSPORT; GENE-EXPRESSION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
48
Recensione:
Indirizzi per estratti:
Indirizzo: Bangs, JD Univ Wisconsin, Sch Med, Dept Med Microbiol & Immunol, 1300 UnivAve, Madison, WI 53706 USA Univ Wisconsin 1300 Univ Ave Madison WI USA 53706 , WI 53706 USA
Citazione:
J.R. Lamb et al., "Functional analysis of the trypanosomal AAA protein TbVCP with trans-dominant ATP hydrolysis mutants", J BIOL CHEM, 276(24), 2001, pp. 21512-21520

Abstract

TbVCP is a member of the AAA ((A) under bar TPases (A) under bar ssociatedwith a variety of cellular (A) under bar ctivities) family of proteins containing two ATPase domains. Southern analysis indicates TbVCP to have a single-locus, two-copy, genomic organization. One copy, but not both, can be disrupted by targeted gene replacement, suggesting that TbVCP is essential for trypanosome viability, Site-directed mutagenesis of the ATP hydrolysis motifs indicates that the second conserved ATPase domain is essential for TbVCP activity. Constitutive overexpression of TbVCP with a single mutation in the second hydrolysis motif or with mutations in both hydrolysis motifs was not possible. Regulated overexpression of these mutants resulted in celldeath as a dominant negative phenotype, In each case cell growth arrested at 24-h post-induction and at all stages of the cell cycle as judged by replication of nuclear and kinetoplast genomes. Onset of growth arrest coincided with the development of severe and characteristic morphological alterations for each mutant. Neither constitutive nor regulated overexpression of wild type TbVCP or the single first hydrolysis domain mutant had any overt effect on cell viability or morphology, However, the distinct phenotype of the double mutant indicates that the first hydrolysis domain, although not essential, does modulate overall TbVCP function. Finally, yeast complementation studies demonstrated that TbVCP can functionally replace the yeast homologue Cdc48p, indicating that protein protein interactions essential to function have been maintained over great phylogenetic distances.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/01/21 alle ore 02:45:19