Dimerization of the DEAD-Box Cyanobacterial RNA Helicase Redox, CrhR

  • Author / Creator
    Skeik, Reem M
  • The DEAD-box cyanobacterial RNA helicase redox, or CrhR, in Synechocystis sp. PCC 6803 is capable of unwinding dsRNA and in annealing ssRNA in a bidirectional ATP-dependent manner. This is a feature shared by only four other DEAD-box RNA helicases. Two of which, the eukaryotic p68 and p72 proteins, were also shown to self-dimerize. Self-dimerization is a characteristic rarely possessed by an RNA helicase. In this study, CrhR was found to exhibit self-interaction using the yeast two-hybrid system and differentially tagged-CrhR protein exchange (swap) analysis, with the dimerization domain localized to the N-terminus, and some assistance, or partial dimerization occurring through the C-terminus. FPLC analysis also revealed CrhR dimerization to occur in an RNA-independent manner. In addition to FPLC analysis, mass spectrometry also suggests CrhR interaction with protein complexes in vivo. These findings suggest physiological functions for CrhR association with ribosomes in multi-subunit complexes upon acclimatization of Synechocystis cells to low temperature.

  • Subjects / Keywords
  • Graduation date
    Fall 2012
  • Type of Item
  • Degree
    Master of Science
  • DOI
  • License
    This thesis is made available by the University of Alberta Libraries with permission of the copyright owner solely for non-commercial purposes. This thesis, or any portion thereof, may not otherwise be copied or reproduced without the written consent of the copyright owner, except to the extent permitted by Canadian copyright law.