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Vol. 12, Issue 12, 3744-3758, December 2001
and
Department of Genetics, Harvard Medical School, Boston
Massachusetts 02115
Hus1, Rad1, and Rad9 are three evolutionarily conserved proteins
required for checkpoint control in fission yeast. These proteins are
known to form a stable complex in vivo. Recently, computational studies
have predicted structural similarity between the individual proteins of
Hus1-Rad1-Rad9 complex and the replication processivity factor
proliferating cell nuclear antigen (PCNA). This has led to the proposal
that the Hus1-Rad1-Rad9 complex may form a PCNA-like ring structure,
and could function as a sliding clamp during checkpoint control. In the
present study, we have attempted to test the predictions of this model
by asking whether the PCNA alignment identifies functionally important
residues or explains mutant phenotypes of hus1,
rad1, or rad9 alleles. Although some of
our results are consistent with the PCNA alignment, others indicate
that the Hus1-Rad1-Rad9 complex possesses unique structural and
functional features.
Exelixis, Inc., 170 Harbor Way, P.O. Box 511, South San Francisco, CA 94083-0511, E-mail
address: ckostrub{at}exelixis.com.
After January 30, 2002, 199 Auburn St., Cambridge,
MA 02139. E-mail address: tlenoch{at}earthlink.net.
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