Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 14, Issue 1, Pages 45-53Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb1180
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Funding
- Intramural NIH HHS Funding Source: Medline
- NCI NIH HHS [CA097096, R01 CA084442] Funding Source: Medline
- NATIONAL CANCER INSTITUTE [R01CA097096] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES [Z01ES065070] Funding Source: NIH RePORTER
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DNA polymerase l (Pol mu) is a family X enzyme with unique substrate specificity that contributes to its specialized role in nonhomologous DNA end joining (NHEJ). To investigate Pol mu's unusual substrate specificity, we describe the 2.4 angstrom crystal structure of the polymerase domain of murine Pol l bound to gapped DNA with a correct dNTP at the active site. This structure reveals substrate interactions with side chains in Pol mu that differ from other family X members. For example, a single amino acid substitution, H329A, has little effect on template-dependent synthesis by Pol mu from a paired primer terminus, but it reduces both template-independent and template-dependent synthesis during NHEJ of intermediates whose 3' ends lack complementary template strand nucleotides. These results provide insight into the substrate specificity and differing functions of four closely related mammalian family X DNA polymerases.
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