The Nuclear Envelope and Spindle Pole Body-Associated Mps3 Protein Bind Telomere Regulators and Function in Telomere Clustering

Lisa M. Antoniacci, Margaret Kenna and Robert V. Skibbens

volume 6 | issue 1

1 January 2007
Pages: 75 - 79

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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 co-precipitations 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.

Authors

Lisa M. Antoniacci

Lehigh University, Bethlehem, PA

Margaret Kenna

Lehigh University, Bethlehem, PA

Robert V. Skibbens

Lehigh University; Bethlehem, PA

We now provide open access to journal articles published online for one year or more. This article may be downloaded at the following link: