Functional characterization of the ubiquitin variant encoded by the baculovirus Autographa californica

Biochemistry
A L HaasL A Guarino

Abstract

The marked evolutionary conservation of ubiquitin is assumed to arise from constraints imposed by folding, stability, and interaction of the polypeptide with various components of the ATP, ubiquitin-dependent degradative pathway. The present studies characterize the most divergent (75% identity) of the species-specific ubiquitin isoforms encoded as a late gene product of the baculovirus Autographa californica [Guarino, L. A. (1990) Proc. Natl. Acad. Sci. U.S.A. 87, 409-413]. Viral ubiquitin supports 40% of the rate of ATP-dependent degradation exhibited by eukaryotic ubiquitin. Inhibition of proteolysis correlated with a lower steady-state concentration of ubiquitin-conjugated degradative intermediates. Rate studies revealed that viral ubiquitin exerts its effect at the step of isopeptide ligase-catalyzed (E3) ubiquitin conjugation since viral and eukaryotic polypeptides are identical in their abilities to support ATP-coupled activation by E1 and transthiolation to E2 carrier proteins. Other studies demonstrated viral ubiquitin severely attenuated the rate of K48-linked multiubiquitin chain formation in E3-independent conjugation catalyzed by recombination yeast CDC34 or rabbit reticulocyte E232K but not chain elongation of alt...Continue Reading

References

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Citations

Sep 2, 2008·The Journal of Microbiology·Xu'ai LinZhifang Zhang
Aug 22, 2007·Trends in Cell Biology·P R Johnson, M Hochstrasser
May 1, 2009·Nature Cell Biology·Felix Randow, Paul J Lehner
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Dec 16, 1998·Journal of Virology·C L AfonsoD L Rock

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