HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Zhaung, Z. P. Articles by McCauley, R. Search for Related Content PubMed PubMed Citation Articles by Zhaung, Z. P. Articles by McCauley, R. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 264, Issue 25, 14594-14596, Sep, 1989

Ubiquitin is involved in the in vitro insertion of monoamine oxidase B into mitochondrial outer membranes

ZP Zhaung and R McCauley
Department of Pharmacology, Wayne State University, Detroit, Michigan 48201.

Monoamine oxidase B that has been synthesized by a reticulocyte lysate charged with bovine liver RNA will insert in a proteinase K-resistant form into isolated outer membranes from rat liver mitochondria. It appears that ubiquitin, a 76-amino acid polypeptide which is enzymatically conjugated to proteins, may be involved in the insertion process. Depletion of endogenous ubiquitin from the reticulocyte lysate with purified antibodies against this polypeptide inhibits the insertion of monoamine oxidase B, and this inhibition is relieved if ubiquitin is restored. On the other hand, a mutant form of ubiquitin which is unable to conjugate with proteins will not support insertion. Conjugation with ubiquitin is an ATP-dependent process. Not only does enzymatic depletion of ATP from the lysate prevent the insertion of monoamine oxidase, but ubiquitin will not restore insertion unless ATP is also present. These data indicate that the formation of a ubiquitin conjugate is involved in the insertion of newly synthesized monoamine oxidase B into the outer membranes.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				A. J. Whitworth, D. A. Theodore, J. C. Greene, H. Benes, P. D. Wes, and L. J. Pallanck Increased glutathione S-transferase activity rescues dopaminergic neuron loss in a Drosophila model of Parkinson's disease PNAS, May 31, 2005; 102(22): 8024 - 8029. [Abstract] [Full Text] [PDF]

				M. S. Lutz, S. R. Ellis, and N. C. Martin Proteasome Mutants, pre4-2 and ump1-2, Suppress the Essential Function but Not the Mitochondrial RNase P Function of the Saccharomyces cerevisiae Gene RPM2 Genetics, March 1, 2000; 154(3): 1013 - 1023. [Abstract] [Full Text]

				H. A. Fisk and M. P. Yaffe A Role for Ubiquitination in Mitochondrial Inheritance in Saccharomyces cerevisiae J. Cell Biol., June 14, 1999; 145(6): 1199 - 1208. [Abstract] [Full Text] [PDF]

				Y. Wang, Y.-G. Yeung, W. Y. Langdon, and E. R. Stanley c-Cbl Is Transiently Tyrosine-phosphorylated, Ubiquitinated, and Membrane-targeted following CSF-1 Stimulation of Macrophages J. Biol. Chem., January 5, 1996; 271(1): 17 - 20. [Abstract] [Full Text] [PDF]

				M. D. Smith, M. Petrak, P. D. Boucher, K. N. Barton, L. Carter, G. Reddy, E. Blachly-Dyson, M. Forte, J. Price, K. Verner, et al. Lysine Residues at Positions 234 and 236 in Yeast Porin Are Involved in Its Assembly into the Mitochondrial Outer Membrane J. Biol. Chem., November 24, 1995; 270(47): 28331 - 28336. [Abstract] [Full Text] [PDF]