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
- Marcin (009) Olszewski,
- Marta Nowak,
- prof. dr hab. Józef Kur link open in new tab
Additional information
- Category
- Inne
- Type
- supllement, wydanie specjalne, dodatek
- Language
- angielski
- Publication year
- 2011
