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Molecular and Cellular Biology, December 2007, p. 8401-8408, Vol. 27, No. 23
0270-7306/07/$08.00+0 doi:10.1128/MCB.01478-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.


Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, Texas 77555-1061,1 Institute of Genetics, Biological Research Center, Hungarian Academy of Sciences, Szeged, Hungary2
Received 15 August 2007/ Returned for modification 6 September 2007/ Accepted 11 September 2007
In Saccharomyces cerevisiae, Rev1 functions in translesion DNA synthesis (TLS) together with polymerase
(Pol
), comprised of the Rev3 catalytic and Rev7 accessory subunits. Rev1 plays an indispensable structural role in promoting Pol
function, and deletion of the Rev1-C terminal region that is involved in physical interactions with Rev3 inactivates Pol
function in TLS. In humans, however, Rev1 has been shown to physically interact with the Y-family polymerases Pol
, Pol
, and Pol
, and the Rev1 C terminus mediates these interactions. Since all the available genetic and biochemical evidence in yeast support the requirement of Rev1 as a structural element for Pol
and not for Pol
, these observations have raised the possibility that in its structural role, Rev1 has diverged between yeast and humans. Here we show that although in yeast a stable Rev1-Pol
complex can be formed, this complex formation involves the polymerase-associated domain of Rev1 and not the Rev1 C terminus as in humans. We also found that the DNA synthesis activity of Rev1 is enhanced in this complex. We discuss the implications of these and other observations for the possible divergence of Rev1's structural role between yeast and humans.
Published ahead of print on 17 September 2007.
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