Literature DB >> 18706966

Streptococcus agalactiae DNA polymerase I is an efficient reverse transcriptase.

Fariborz Bahrami1, Jean-Luc Jestin.   

Abstract

Genome annotations result generally from large sequence alignments by bioinformatics. Large scale biochemical data are more difficult to obtain. They derive for example from directed protein evolution experiments by selection. A previously reported directed enzyme evolution experiment by in vitro selection of Stoffel fragment variants of Taq DNA polymerase I was used here to predict the activities of Streptococcus agalactiae DNA polymerase I. The reverse transcriptase activity of S. agalactiae DNA polymerase I was measured and the kinetic parameters for this RNA-dependent DNA polymerase are given. RNA-templated DNA repair is suggested as a possible biological function for this biochemical activity.

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Year:  2008        PMID: 18706966     DOI: 10.1016/j.biochi.2008.07.006

Source DB:  PubMed          Journal:  Biochimie        ISSN: 0300-9084            Impact factor:   4.079


  3 in total

1.  Characterisation of a DNA polymerase highly mutated along the template binding interface.

Authors:  Sophie Vichier-Guerre; Jean-Luc Jestin
Journal:  Mol Biotechnol       Date:  2010-09       Impact factor: 2.695

Review 2.  Optimization models and the structure of the genetic code.

Authors:  J L Jestin; A Kempf
Journal:  J Mol Evol       Date:  2009-10-20       Impact factor: 2.395

Review 3.  Tailor-made biocatalysts: combining thermodynamics, organic synthesis, molecular biology, biochemistry and microbiology for the design of enzyme selections.

Authors:  Jean-Luc Jestin
Journal:  Comput Struct Biotechnol J       Date:  2012-10-28       Impact factor: 7.271

  3 in total

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