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Novel primosomal protein B from thermophilic bacterium Thermoanerobacter tengcongensis

Abstract

We report the identification and characterization of theprimosomal protein B (PriB) from thermophilic bacteriumThermoanerobacter tengcongensis (TtePriB). It is the largestknown bacterial PriB protein consisting 216 amino acidresidues with a calculated molecular mass of 25 kDa. Surprisingly,it is functional as monomer containing two single-stranded DNA binding domain (OB-fold) and it is thecompletely new kind structure of SSB protein. BacterialSSBs proteins identified to date are homodimers (e.g. PriBfrom Escherichia coli) or monomers (e.g. PriB from Klebsiellapnuemoniae).The ssDNA-binding site for TtePriB is 34±2 nucleotideslong as shown by using fluorescence spectroscopy. Thehalf-lives of TtePriB was 10 min at 75°C. These resultsshowed that TtePriB as the first characterized PriB fromthermophilic microorganizm is thermostable primosomalprotein B with unique structure, offering an attractive alternativefor other thermostable proteins with two OB-foldsper monomer (TaqSSB and TthSSB) in their applicationsfor molecular biology techniques.

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Category:
Other
Type:
supllement, wydanie specjalne, dodatek
Published in:
Acta Biochimica Polonica no. 58,
ISSN: 0001-527X
Title of issue:
Acta Biochimica Polonica.
Language:
English
Publication year:
2011
Bibliographic description:
Olszewski M., Nowak M., Kur J.:Novel primosomal protein B from thermophilic bacterium Thermoanerobacter tengcongensis//.-Vol. 58,nr. suppl. 2(2011),
Verified by:
Gdańsk University of Technology

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