An interplay between Centrin2 and Centrin4 on the bi-lobed structure in Trypanosoma brucei

Mol Microbiol. 2012 Mar;83(6):1153-61. doi: 10.1111/j.1365-2958.2012.07998.x. Epub 2012 Feb 13.

Abstract

Centrins are conserved calcium-binding proteins important for various regulatory functions. In procyclic Trypanosoma brucei, TbCentrin2 and TbCentrin4 have distinct effects on cell division but both localize to the basal bodies that seed the flagellum, and a bi-lobed structure important for organelle duplication and cell division. Here we show that TbCentrin2 and TbCentrin4 both bind to the basal bodies and bi-lobed structure through the conserved C-terminal domain. Molecular genetic manipulation of TbCentrin4 levels greatly affects TbCentrin2 association with the bi-lobed structure. Using established synchronization methods, TbCentrin2 expression level is shown to be relatively constant throughout the cell cycle while TbCentrin4 level fluctuates, decreasing most during early S-phase when the bi-lobe undergoes duplication. These results thus suggest a co-ordinated action between these two centrin proteins, where the cell cycle-dependent TbCentrin4 expression could regulate the abundance of TbCentrin2 on the bi-lobed structure.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Calcium-Binding Proteins / chemistry
  • Calcium-Binding Proteins / genetics
  • Calcium-Binding Proteins / metabolism*
  • Cell Cycle
  • Cell Polarity
  • Protein Structure, Tertiary
  • Protozoan Proteins / chemistry
  • Protozoan Proteins / genetics
  • Protozoan Proteins / metabolism*
  • Trypanosoma brucei brucei / chemistry
  • Trypanosoma brucei brucei / cytology
  • Trypanosoma brucei brucei / genetics
  • Trypanosoma brucei brucei / metabolism*

Substances

  • Calcium-Binding Proteins
  • Protozoan Proteins