Kleisins: A Superfamily of Bacterial and Eukaryotic SMC Protein Partners

Mol Cell. 2003 Mar;11(3):571-5. doi: 10.1016/s1097-2765(03)00108-4.

Abstract

We describe a superfamily of eukaryotic and prokaryotic proteins (kleisins) that includes ScpA, Scc1, Rec8, and Barren. Scc1 interacts with SMC proteins through N- and C-terminal domains to form a ring-like structure. Since these are the only domains conserved among kleisins, we suggest that ring formation with SMC proteins may define this family.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / physiology
  • Adhesins, Bacterial*
  • Amino Acid Sequence
  • Animals
  • Bacterial Proteins / physiology*
  • Cell Cycle Proteins / physiology*
  • Chromosomal Proteins, Non-Histone
  • DNA-Binding Proteins / physiology
  • Drosophila Proteins*
  • Endopeptidases / physiology*
  • Fungal Proteins
  • Humans
  • Molecular Sequence Data
  • Multigene Family
  • Multiprotein Complexes
  • Nuclear Proteins / chemistry
  • Phosphoproteins / physiology*
  • Protein Binding
  • Protein Structure, Tertiary
  • Saccharomyces cerevisiae Proteins
  • Schizosaccharomyces pombe Proteins / physiology*
  • Sequence Homology, Amino Acid

Substances

  • Adhesins, Bacterial
  • Bacterial Proteins
  • Barr protein, Drosophila
  • Cell Cycle Proteins
  • Chromosomal Proteins, Non-Histone
  • DNA-Binding Proteins
  • Drosophila Proteins
  • Fungal Proteins
  • MCD1 protein, S cerevisiae
  • Multiprotein Complexes
  • Nuclear Proteins
  • Phosphoproteins
  • Saccharomyces cerevisiae Proteins
  • Schizosaccharomyces pombe Proteins
  • cohesins
  • condensin complexes
  • psm1 protein, S pombe
  • REC8 protein, S pombe
  • Endopeptidases
  • C5a peptidase
  • Adenosine Triphosphatases