English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Background  In recent years, there has been an increasing interest in SSBs because they find numerous applications in diverse molecular biology and analytical methods.    Results  We report the characterization of single-stranded DNA binding proteins (SSBs) from the thermophilic bacteria  Thermotoga maritima  ( Tma SSB) and  Thermotoga neapolitana  ( Tne SSB). They are the smallest known bacterial SSB proteins, consisting of 141 and 142 amino acid residues with a calculated molecular mass of 16.30 and 16.58 kDa, respectively. The similarity between amino acid sequences of these proteins is very high: 90% identity and 95% similarity. Surprisingly, both  Tma SSB and  Tne SSB possess a quite low sequence similarity to  Escherichia coli  SSB (36 and 35% identity, 55 and 56% similarity, respectively). They are functional as homotetramers containing one single-stranded DNA binding domain (OB-fold) in each monomer. Agarose mobility assays indicated that the ssDNA-binding site for both proteins is salt independent, and fluorescence spectroscopy resulted in a size of 68 ± 2 nucleotides. The half-lives of  Tma SSB and  Tne SSB were 10 h and 12 h at 100°C, respectively. When analysed by differential scanning microcalorimetry (DSC) the melting temperature ( T  m ) was 109.3°C and 112.5°C for  Tma SSB and  Tne SSB, respectively.    Conclusion  The results showed that  Tma SSB and  Tne SSB are the most thermostable SSB proteins identified to date, offering an attractive alternative to  Taq SSB and  Tth SSB in molecular biology applications, especially with using high temperature e. g. polymerase chain reaction (PCR).

Characterization of exceptionally thermostable single-stranded DNA-binding proteins from Thermotoga maritima and Thermotoga neapolitana