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.
Authors (3)
Cite as
Full text
full text is not available in portal
Keywords
Details
- 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
seen 107 times
Recommended for you
Novel DNA-binding protein from Nanoarchaeum equitans Kin4-M binds all kinds of nucleic acids
- M. (. Olszewski,
- J. Balsewicz,
- M. Nowak
- + 1 authors
Novel single-stranded DNA-binding protein from psyvhrophilic bacterium Psychrobacter arcticus
- M. Nowak,
- M. (. Olszewski,
- J. Kur