JCB logo
Accuri Cytometers
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents

Published online 23 February 2004. doi:10.1083/jcb.200308012
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 164, Number 5, 677-688
This Article
Right arrow Full Text
Right arrow PDF (Full Text)
Right arrow PPT slides of all figures
Right arrow Supplemental Material Index
Right arrow Alert me when this article is cited
Right arrow Citation Map
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Youngman, M. J.
Right arrow Articles by Jensen, R. E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Youngman, M. J.
Right arrow Articles by Jensen, R. E.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Article

Mmm2p, a mitochondrial outer membrane protein required for yeast mitochondrial shape and maintenance of mtDNA nucleoids

Matthew J. Youngman, Alyson E. Aiken Hobbs, Shawn M. Burgess, Maithreyan Srinivasan, and Robert E. Jensen

Department of Cell Biology, The Johns Hopkins University School of Medicine, Baltimore, MD 21205

Address correspondence to Robert E. Jensen, Department of Cell Biology, Johns Hopkins University School of Medicine, 725 N. Wolfe St., Baltimore, MD 21205. Tel.: (410) 955-7291. Fax: (410) 955-7293. email: rjensen{at}jhmi.edu

The mitochondrial outer membrane protein, Mmm1p, is required for normal mitochondrial shape in yeast. To identify new morphology proteins, we isolated mutations incompatible with the mmm1-1 mutant. One of these mutants, mmm2-1, is defective in a novel outer membrane protein. Lack of Mmm2p causes a defect in mitochondrial shape and loss of mitochondrial DNA (mtDNA) nucleoids. Like the Mmm1 protein (Aiken Hobbs, A.E., M. Srinivasan, J.M. McCaffery, and R.E. Jensen. 2001. J. Cell Biol. 152:401–410.), Mmm2p is located in dot-like particles on the mitochondrial surface, many of which are adjacent to mtDNA nucleoids. While some of the Mmm2p-containing spots colocalize with those containing Mmm1p, at least some of Mmm2p is separate from Mmm1p. Moreover, while Mmm2p and Mmm1p both appear to be part of large complexes, we find that Mmm2p and Mmm1p do not stably interact and appear to be members of two different structures. We speculate that Mmm2p and Mmm1p are components of independent machinery, whose dynamic interactions are required to maintain mitochondrial shape and mtDNA structure.

Key Words: mitochondrial morphology; mtDNA nucleoids; outer membrane protein


A.E. Aiken Hobbs and S.M. Burgess made equal contributions to this work.

The online version of this article contains supplemental material.

S.M. Burgess's present address is National Human Genome Research Group, Building 50, Room 5537, 50 South Dr., MSC 8004, Bethesda, MD 20892-8004.

M. Srinivasan's present address is 454 Life Sciences, 20 Commercial St., Bradford, CT 06405.

Abbreviations used in this paper: DIC, differential interference contrast; mtDNA, mitochondrial DNA; RFP, red fluorescent protein; TEV, tobacco etch virus.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:



  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents