Molecular analyses of an unusual translesion DNA polymerase from Methanosarcina acetivorans C2A
| Autor: | Claudia E. Guzman, Shigenori Iwai, Shou Mei, Yi Hsing Chen, Li Jung Lin, Roderick I. Mackie, Aya Yoshinaga, Isaac K. O. Cann, Yoshizumi Ishino, Angelica M. Lagunas, Satish K. Nair, Satoshi Koike, Yuyen Lin, M. Ashley Spies |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
DNA polymerase
Archaeal Proteins Amino Acid Motifs Molecular Sequence Data Pyrimidine dimer DNA-Directed DNA Polymerase Structural Biology Crenarchaeota Proliferating Cell Nuclear Antigen PCNA Humans Amino Acid Sequence Methanosarcina acetivorans translesion DNA synthesis Molecular Biology Polymerase Phylogeny DNA Primers Genetics biology Sequence Homology Amino Acid Adenine family Y polymerase biology.organism_classification Archaea Sulfolobus DinB DNA Archaeal Biochemistry Multigene Family Methanosarcina Mutation biology.protein Euryarchaeota Sequence Alignment DNA Damage Protein Binding |
| Zdroj: | Journal of molecular biology. 397(1) |
| ISSN: | 1089-8638 |
| Popis: | The domain Archaea is composed of several subdomains, and prominent among them are the Crenarchaeota and the Euryarchaeota. Biochemically characterized archaeal family Y DNA polymerases (Pols) or DinB homologs, to date, are all from crenarchaeal organisms, especially the genus Sulfolobus. Here, we demonstrate that archaeal family Y Pols fall into five clusters based on phylogenetic analysis. MacDinB-1, the homolog from the euryarchaeon Methanosarcina acetivorans that is characterized in this study, belongs to cluster II. Therefore, MacDinB-1 is different from the Sulfolobus DinB proteins, which are members of cluster I. In addition to translesion DNA synthesis activity, MacDinB-1 synthesized unusually long products ( approximately 7.2 kb) in the presence of its cognate proliferating cell nuclear antigen (PCNA). The PCNA-interacting site in MacDinB-1 was identified by mutational analysis in a C-terminally located heptapeptide akin to a PIP (PCNA-interacting protein) box. In vitro assays from the present report suggested that MacDinB-1 works in an error-free mode to repair cyclobutane pyrimidine dimers. This study on a euryarchaeal DinB homolog provides important insights into the functional diversity of the family Y Pols, and the availability of a genetic system for this archaeon should allow subsequent elucidation of the physiological significance of this enzyme in M. acetivorans cells. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect