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A gradient of template dependence defines distinct biological roles for family X polymerases in nonhomologous end joining.
- S. A. Nick McElhinny, Jody M. Havener, +6 authors D. Ramsden
- Biology, Medicine
- Molecular cell
- 5 August 2005
It is shown here that pol mu and pol lambda are similarly recruited by NHEJ factors to fill gaps when ends have partially complementary overhangs, suggesting equivalent roles promoting accuracy in N HEJ. Expand
Plastid gene expression and plant development require a plastidic protein of the mitochondrial transcription termination factor family
- E. Babiychuk, K. Vandepoele, +9 authors S. Kushnir
- Medicine, Biology
- Proceedings of the National Academy of Sciences
- 4 April 2011
Overall, the results indicate that biosynthesis of malonyl-CoA and plastid-derived systemic growth-promoting compounds are the processes that link plant development and plastsid gene expression. Expand
DNA polymerase mu (Pol μ), homologous to TdT, could act as a DNA mutator in eukaryotic cells
Interestingly, unlike TdT, the catalytic efficiency of polymerization carried out by Pol μ was enhanced by the presence of a template strand, leading to the preferred insertion of complementary nucleotides, although with low discrimination values. Expand
DNA polymerase lambda (Pol lambda), a novel eukaryotic DNA polymerase with a potential role in meiosis.
First evidences suggest a potential role of Pol lambda in DNA repair synthesis associated with meiosis, and conserves the critical residues of Pol beta required for its intrinsic deoxyribose phosphate lyase (dRPase) activity. Expand
Helix Unwinding and Base Flipping Enable Human MTERF1 to Terminate Mitochondrial Transcription
- E. Yakubovskaya, Edison Mejía, J. Byrnes, Elena Hambardjieva, M. García-Díaz
- Biology, Medicine
- 11 June 2010
The structure of a member of this family, the human mitochondrial transcriptional terminator MTERF1, bound to dsDNA containing the termination sequence is solved and it is demonstrated that upon sequence recognition MterF1 unwinds the DNA molecule, promoting eversion of three nucleotides. Expand
Implication of DNA Polymerase λ in Alignment-based Gap Filling for Nonhomologous DNA End Joining in Human Nuclear Extracts*
- J. Lee, L. Blanco, +5 authors L. Povirk
- Biology, Medicine
- Journal of Biological Chemistry
- 2 January 2004
The results suggest that polymerase λ is the primary gap-filling polymerase for accurate nonhomologous end joining, and that the Brca1 C-terminal domain is required for this activity. Expand
Structural insight into the substrate specificity of DNA Polymerase mu.
This work describes the crystal structure of the polymerase domain of murine Pol mu bound to gapped DNA with a correct dNTP at the active site and reveals substrate interactions with side chains in Pol mu that differ from other family X members. Expand
DNA polymerase lambda (Pol λ), a novel eukaryotic DNA polymerase with a potential role in meiosis.
Northern blotting, in situ hybridizationanalysis and immunostaining showed high levels of Pol l speciﬁcally expressed in testis, being developmentally regulated and mainly associ-ated to pachytene spermatocytes, suggesting a potential role ofPol l in DNA repair synthesis associated withmeiosis. Expand
Identification of an Intrinsic 5′-Deoxyribose-5-phosphate Lyase Activity in Human DNA Polymerase λ
- M. García-Díaz, K. Bębenek, T. Kunkel, L. Blanco
- Biology, Chemistry
- The Journal of Biological Chemistry
- 14 September 2001
The dRP lyase activity of Pol λ, in coordination with its polymerization activity, efficiently repaired uracil-containing DNA in an in vitroconstituted BER reaction, suggesting that Pol κ may participate in “single-nucleotide” base excision repair in mammalian cells. Expand
The X family portrait: structural insights into biological functions of X family polymerases.
This work considers how distinctive structural features of these enzymes contribute to their biological functions in vivo, making this the first mammalian polymerase family whose structural portrait is complete. Expand