title: DNA polymerase lambda (Pol lambda), a novel eukaryotic DNA polymerase with a potential role in meiosis.
abstract: A new gene (POLL) encoding a novel DNA polymerase (Pol lambda) has been identified at mouse chromosome 19. Murine Pol lambda, consisting of 573 amino acid residues, has a 32% identity to Pol beta, involved in nuclear DNA repair in eukaryotic cells. It is interesting that Pol lambda contains all the critical residues involved in DNA binding, nucleotide binding and selection, and catalysis of DNA polymerization, that are conserved in Pol beta and other DNA polymerases belonging to family X. Murine Pol lambda, overproduced in Escherichia coli, displayed intrinsic DNA polymerase activity when assessed by in situ gel analysis. Pol lambda also conserves the critical residues of Pol beta required for its intrinsic deoxyribose phosphate lyase (dRPase) activity. The first 230 amino acid residues of Pol lambda, that have no counterpart in Pol beta, contain a BRCT domain, present in a variety of cell-cycle check-point control proteins responsive to DNA damage and proteins involved in DNA repair. Northern blotting, in situ hybridization analysis and immunostaining showed high levels of Pol lambda specifically expressed in testis, being developmentally regulated and mainly associated to pachytene spermatocytes. These first evidences, although indirect, suggest a potential role of Pol lambda in DNA repair synthesis associated with meiosis.
authors.affiliation: Centro de Biología Molecular Severo Ochoa (CSIC-UAM), Universidad Autónoma, Madrid, 28049, Spain.
authors.forename: M
authors.initials: M
authors.lastname: García-Díaz
authors.forename: O
authors.initials: O
authors.lastname: Domínguez
authors.forename: L A
authors.initials: LA
authors.lastname: López-Fernández
authors.forename: L T
authors.initials: LT
authors.lastname: de Lera
authors.forename: M L
authors.initials: ML
authors.lastname: Saníger
authors.forename: J F
authors.initials: JF
authors.lastname: Ruiz
authors.forename: M
authors.initials: M
authors.lastname: Párraga
authors.forename: M J
authors.initials: MJ
authors.lastname: García-Ortiz
authors.forename: T
authors.initials: T
authors.lastname: Kirchhoff
authors.forename: J
authors.initials: J
authors.lastname: del Mazo
authors.forename: A
authors.initials: A
authors.lastname: Bernad
authors.forename: L
authors.initials: L
authors.lastname: Blanco
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D003001:Cloning, Molecular; D017124:Conserved Sequence; D019951:DNA Polymerase beta / Q000737:chemistry / Q000378:metabolism; D004260:DNA Repair; D004259:DNA-Directed DNA Polymerase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D005057:Eukaryotic Cells / Q000166:cytology / Q000201:enzymology*; D005091:Exons / Q000235:genetics; D018507:Gene Expression Regulation, Developmental; D015971:Gene Expression Regulation, Enzymologic; D006801:Humans; D007438:Introns / Q000235:genetics; D008297:Male; D008540:Meiosis / Q000235:genetics; D051379:Mice; D008810:Mice, Inbred C57BL; D008954:Models, Biological; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D012333:RNA, Messenger / Q000032:analysis / Q000235:genetics; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D016415:Sequence Alignment; D013087:Spermatids / Q000201:enzymology; D013090:Spermatocytes / Q000201:enzymology; D013737:Testis / Q000166:cytology / Q000201:enzymology / Q000378:metabolism
chemical_list: D012333:RNA, Messenger; D019951:DNA Polymerase beta; D004259:DNA-Directed DNA Polymerase