The nuclear envelope and spindle pole body-associated Mps3 protein bind telomere regulators and function in telomere clustering

Cell Cycle. 2007 Jan 1;6(1):75-9. doi: 10.4161/cc.6.1.3647. Epub 2007 Jan 27.

Abstract

It has long been posited that the nuclear envelope is a key regulator of both the spatial organization of chromatin and gene transcription. Mps3p is an integral nuclear envelope membrane protein with a single trans-membrane domain that is essential for spindle pole body duplication. More recently, Mps3p was shown to associate with the cohesion establishment factor Ctf7p and found to be critical for cohesion establishment. Here, we provide new evidence that the nuclear envelope, via Mps3p, plays a pivotal role in telomere foci formation. Results from in vitro pull-downs and in vivo coprecipitations also show that Mps3p associates with the telomerase-assembly component Est1p. Moreover, pair-wise combinations of mps3, est1 or ctf7 alleles all produce conditional lethality. Findings that Mps3p and the nuclear envelope recruit/sequester soluble chromatin metabolism factors such as Ctf7p and Est1p describe, at the molecular level, a new mechanism of nuclear envelope-dependent chromatin regulation.

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • Membrane Proteins / physiology
  • Nuclear Envelope / genetics
  • Nuclear Envelope / metabolism*
  • Nuclear Envelope / physiology
  • Nuclear Proteins
  • Protein Binding / genetics
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / metabolism*
  • Saccharomyces cerevisiae Proteins / physiology
  • Spindle Apparatus / genetics
  • Spindle Apparatus / metabolism*
  • Telomere / genetics
  • Telomere / metabolism*
  • Telomere-Binding Proteins / genetics
  • Telomere-Binding Proteins / metabolism*
  • Telomere-Binding Proteins / physiology

Substances

  • Membrane Proteins
  • Mps3 protein, S cerevisiae
  • Nuclear Proteins
  • Saccharomyces cerevisiae Proteins
  • Telomere-Binding Proteins