Skip NavigationSkip to Content
Return Return to Search Results

Solution structure, domain features, and structural implications of mutants of the chromo domain from the fission yeast histone methyltransferase Clr4

  1. Author:
    Horita, D. A.
    Ivanova, A. V.
    Altieri, A. S.
    Klar, A. J. S.
    Byrd, R. A.

  2. Author Address

    Wake Forest Univ, Sch Med, Dept Biochem, Med Ctr Blvd, Winston Salem, NC 27157 USA. NCI, Struct Biophys Lab, Frederick, MD 21702 USA. NCI, Gene Regulat & Chromosome Biol Lab, Frederick, MD 21702 USA. Horita DA Wake Forest Univ, Sch Med, Dept Biochem, Med Ctr Blvd, Winston Salem, NC 27157 USA.
    1. Year: 2001
  2. Journal: Journal of Molecular Biology
    1. 307
    2. 3
    3. Pages: 861-870
  4. Type of Article: Article
  1. Abstract:

    The encapsulation of otherwise transcribable loci within transcriptionally inactive heterochromatin is rapidly gaining recognition as an important mechanism of epigenetic gene regulation. In the fission yeast Schizosaccharomyces pombe, heterochromatinization of the mat2/mat3 loci silences the mating-type information encoded within these loci. Here, we present the solution structure of the chromo domain from the cryptic loci regulator protein Clr4. Clr4 is known to regulate silencing and switching at the mating-type loci and to affect chromatin structure at centromeres. Clr3 and its human and Drosophila homologs have been identified as histone MS-specific methyltransferases, further implicating this family of proteins in chromatin remodeling. Our structure highlights a conserved surface that may be involved in chrome domain-ligand interactions. We have also analyzed two chrome domain mutants (W31G and W41G) that previously were shown to affect silencing and switching in full-length Clr4. Both mutants are significantly destabilized relative to wild-type. (C) 2001 Academic Press.

    See More

  1. Keywords:

External Sources

  1. No sources found.

Library Notes

  1. No notes added.
NCI at Frederick

You are leaving a government website.

This external link provides additional information that is consistent with the intended purpose of this site. The government cannot attest to the accuracy of a non-federal site.

Linking to a non-federal site does not constitute an endorsement by this institution or any of its employees of the sponsors or the information and products presented on the site. You will be subject to the destination site's privacy policy when you follow the link.

ContinueCancel