Localization of self-interacting domains within betaretrovirus Gag polyproteins

. 2005 Feb 20 ; 332 (2) : 659-66.

Jazyk angličtina Země Spojené státy americké Médium print

Typ dokumentu časopisecké články, práce podpořená grantem, Research Support, U.S. Gov't, P.H.S.

Perzistentní odkaz   https://www.medvik.cz/link/pmid15680431

Grantová podpora
R01 AI043230-05 NIAID NIH HHS - United States
R01AI43230 NIAID NIH HHS - United States

Odkazy

PubMed 15680431
DOI 10.1016/j.virol.2004.12.007
PII: S0042-6822(04)00838-4
Knihovny.cz E-zdroje

The Betaretrovirus genus is characterized by the ability to preassemble immature capsids within the cytoplasm. For Mason-Pfizer monkey virus (M-PMV) this ability depends in part upon the unique Internal Scaffold Domain (ISD) within the p12 region of Gag. In this study, we have further characterized the ability of M-PMV p12 to promote Gag-Gag interaction and have examined the Gag polyprotein of the related mouse mammary tumor virus (MMTV) to potentially identify a region with equivalent function. Using the yeast two-hybrid system, we confirmed that both Gag polyproteins strongly interact, primarily through the CA-NC regions, but also through additional domains N-terminal to CA. For M-PMV, this auxiliary interaction domain was p12. For MMTV, no single strongly self-interacting protein was identified. Instead, MMTV Gag appears to utilize the weak contributions of several protein domains to support the main interaction of its CA-NC. Our findings suggest that, in addition to the canonical NC "I-domain" interaction, MMTV Gag self-association results from the concerted action of multiple regions of the polyprotein while M-PMV Gag relies mainly on its p12 domain.

Citace poskytuje Crossref.org

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