JCB logo
Quantitative Colocalization Analysis Software
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents

This Article
Right arrow Full Text
Right arrow Full Text (PDF, 218K)
Right arrow PPT slides of all figures
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 CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Snyder, W. B.
Right arrow Articles by Subramani, S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Snyder, W. B.
Right arrow Articles by Subramani, S.
Right arrowPubmed/NCBI databases
*Substance via MeSH
Related Collections
Right arrowRelated Article
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Facebook   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?

© The Rockefeller University Press, 0021-9525/2000//1171 $5.00
The Journal of Cell Biology, Volume 149, Number 6, , 2000 1171-1178


Brief Report

The Peroxin Pex19p Interacts with Multiple, Integral Membrane Proteins at the Peroxisomal Membrane



William B. Snydera, Antonius Kollera, A. Jobu Choya, and Suresh Subramania

a Department of Biology, University of California, San Diego, La Jolla, California 92093-0322
Department of Biology, University of California, San Diego, 3230 Bonner Hall, 9500 Gilman Drive, La Jolla, CA 92093-0322.(858) 534-0053(858) 534-2327

ssubramani{at}ucsd.edu

Pex19p is a protein required for the early stages of peroxisome biogenesis, but its precise function and site of action are unknown. We tested the interaction between Pex19p and all known Pichia pastoris Pex proteins by the yeast two-hybrid assay. Pex19p interacted with six of seven known integral peroxisomal membrane proteins (iPMPs), and these interactions were confirmed by coimmunoprecipitation. The interactions were not reduced upon inhibition of new protein synthesis, suggesting that they occur with preexisting, and not newly synthesized, pools of iPMPs. By mapping the domains in six iPMPs that interact with Pex19p and the iPMP sequences responsible for targeting to the peroxisome membrane (mPTSs), we found the majority of these sites do not overlap. Coimmunoprecipitation of Pex19p from fractions that contain peroxisomes or cytosol revealed that the interactions between predominantly cytosolic Pex19p and the iPMPs occur in the organelle pellet that contains peroxisomes. These data, taken together, suggest that Pex19p may have a chaperone-like role at the peroxisome membrane and that it is not the receptor for targeting of iPMPs to the peroxisome.

Key Words: organelle biogenesis • protein localization • peroxin • chaperone • mPTS receptor



© 2000 The Rockefeller University Press

W.B. Snyder and A. Koller contributed equally to this paper.

Abbreviations used in this paper: DSP, dithiobis(succinimidyl propionate); GFP, green fluorescent protein; iPMP(s), integral peroxisome membrane protein(s); mPTS(s), integral peroxisome membrane protein targeting signal(s); PTS(s), peroxisome targeting signal(s).



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 Facebook Facebook   Add to Reddit Reddit   Add to Technorati Technorati   Add to Twitter Twitter    What's this?

Related Article


J. Cell Biol. 2000 149: 1-2. [Full Text] [PDF]





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