TY - JOUR
T1 - Separate roles of structured and unstructured regions of Y-family DNA polymerases.
AU - Ohmori, Haruo
AU - Hanafusa, Tomo
AU - Ohashi, Eiji
AU - Vaziri, Cyrus
N1 - Funding Information:
We thank Katsuhiko Sasaki for his excellent technical assistance and also Junya Tomida and Takeshi Todo for permitting us to cite their unpublished results. Our works described and cited here were supported by grants-in-aids (17013041 to H. O.) from the Ministry of Education, Sports, Science, and Technology of Japan and by grants (ES09558 to C. V.) from the National Institutes of Health, USA.
PY - 2009
Y1 - 2009
N2 - All organisms have multiple DNA polymerases specialized for translesion DNA synthesis (TLS) on damaged DNA templates. Mammalian TLS DNA polymerases include Pol eta, Pol iota, Pol kappa, and Rev1 (all classified as "Y-family" members) and Pol zeta (a "B-family" member). Y-family DNA polymerases have highly structured catalytic domains; however, some of these proteins adopt different structures when bound to DNA (such as archaeal Dpo4 and human Pol kappa), while others maintain similar structures independently of DNA binding (such as archaeal Dbh and Saccharomyces cerevisiae Pol eta). DNA binding-induced structural conversions of TLS polymerases depend on flexible regions present within the catalytic domains. In contrast, noncatalytic regions of Y-family proteins, which contain multiple domains and motifs for interactions with other proteins, are predicted to be mostly unstructured, except for short regions corresponding to ubiquitin-binding domains. In this review we discuss how the organization of structured and unstructured regions in TLS polymerases is relevant to their regulation and function during lesion bypass.
AB - All organisms have multiple DNA polymerases specialized for translesion DNA synthesis (TLS) on damaged DNA templates. Mammalian TLS DNA polymerases include Pol eta, Pol iota, Pol kappa, and Rev1 (all classified as "Y-family" members) and Pol zeta (a "B-family" member). Y-family DNA polymerases have highly structured catalytic domains; however, some of these proteins adopt different structures when bound to DNA (such as archaeal Dpo4 and human Pol kappa), while others maintain similar structures independently of DNA binding (such as archaeal Dbh and Saccharomyces cerevisiae Pol eta). DNA binding-induced structural conversions of TLS polymerases depend on flexible regions present within the catalytic domains. In contrast, noncatalytic regions of Y-family proteins, which contain multiple domains and motifs for interactions with other proteins, are predicted to be mostly unstructured, except for short regions corresponding to ubiquitin-binding domains. In this review we discuss how the organization of structured and unstructured regions in TLS polymerases is relevant to their regulation and function during lesion bypass.
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U2 - 10.1016/s1876-1623(08)78004-0
DO - 10.1016/s1876-1623(08)78004-0
M3 - Review article
C2 - 20663485
AN - SCOPUS:78049441698
SN - 1876-1623
VL - 78
SP - 99
EP - 146
JO - Advances in protein chemistry and structural biology
JF - Advances in protein chemistry and structural biology
ER -