Towards understanding cell cycle control in Cryptococcus neoformans: structure-function relationship of G1 and G1/S cyclins homologue CnCln1

Biochem Biophys Res Commun. 2011 Dec 9;416(1-2):217-21. doi: 10.1016/j.bbrc.2011.11.040. Epub 2011 Nov 15.

Abstract

We have previously reported that only a single Cdk1-related G1 and G1/S cyclin homologue was found in the genome sequence of the pathogenic basidiomycetous yeast Cryptococcus neoformans (C. neoformans) and designated it CnCln1. Surprisingly, CnCln1 was not only able to complement the function of the G1 cyclins of the ascomycetous budding yeast Saccharomyces cerevisiae (S. cerevisiae), such as ScCln3, but also the G1/S cyclins of S. cerevisiae, such as ScCln1 and ScCln2. In this study, we investigated how CnCln1 cooperates with the cyclin-dependent kinases of S. cerevisiae (ScCdk1) and substitutes the function of G1 and G1/S cyclins of S. cerevisia from a point of view of their structure-function relationship. Our in silico analysis demonstrated that the CnCln1/ScCdk1 complex was more stable than any of the yeast cyclin and ScCdk1complexes. Thus, these results are consistent with in vitro analysis that has revealed the flexible functional capacity of CnCln1 as a Cdk1-related G1 and G1/S cyclins of S. cerevisiae.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Cell Cycle*
  • Cryptococcus neoformans / cytology
  • Cryptococcus neoformans / physiology*
  • Cyclins / chemistry
  • Cyclins / genetics
  • Cyclins / metabolism*
  • G1 Phase
  • Genetic Complementation Test
  • Molecular Sequence Data
  • Protein Conformation
  • S Phase
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / physiology
  • Structure-Activity Relationship

Substances

  • Cyclins