Experts and Doctors on thermus in New York, United States


Locale: New York, United States
Topic: thermus

Top Publications

  1. Lamour V, Hogan B, Erie D, Darst S. Crystal structure of Thermus aquaticus Gfh1, a Gre-factor paralog that inhibits rather than stimulates transcript cleavage. J Mol Biol. 2006;356:179-88 pubmed
    ..The latter two characteristics suggest that Gfh1 chelates a magnesium ion in the RNA polymerase active site (like GreA) but in a catalytically inactive configuration. ..
  2. Feklistov A, Darst S. Crystallographic analysis of an RNA polymerase σ-subunit fragment complexed with -10 promoter element ssDNA: quadruplex formation as a possible tool for engineering crystal contacts in protein-ssDNA complexes. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013;69:950-5 pubmed publisher
    ..Here, a new crystal form is presented with a different arrangement of G-columns and it is proposed that the fortuitous finding of G-quartet packing could be useful in engineering crystal contacts in protein-ssDNA complexes. ..
  3. Murakami K, Darst S. Bacterial RNA polymerases: the wholo story. Curr Opin Struct Biol. 2003;13:31-9 pubmed
    ..Comparisons with structural analyses of evolutionarily unrelated RNA polymerases reveal unexpected general features of the initiation process. ..
  4. Weixlbaumer A, Leon K, Landick R, Darst S. Structural basis of transcriptional pausing in bacteria. Cell. 2013;152:431-41 pubmed publisher
    ..Our results provide a framework for understanding how RNA hairpin formation stabilizes the paused state and how the ePEC intermediate facilitates termination...
  5. Tong J, Cao W, Barany F. Biochemical properties of a high fidelity DNA ligase from Thermus species AK16D. Nucleic Acids Res. 1999;27:788-94 pubmed
    ..Both Thermus ligases exhibit enhanced mismatch ligation when Mn2+is substituted for Mg2+, but the Tsp. AK16D ligase remains more specific toward perfectly matched substrate...
  6. Murakami K, Masuda S, Darst S. Structural basis of transcription initiation: RNA polymerase holoenzyme at 4 A resolution. Science. 2002;296:1280-4 pubmed publisher
    ..The advancing RNA transcript must displace the loop, leading to abortive initiation and ultimately to sigma release...
  7. Feklistov A, Darst S. Structural basis for promoter-10 element recognition by the bacterial RNA polymerase ? subunit. Cell. 2011;147:1257-69 pubmed publisher
    ..These results provide a detailed structural basis for the critical roles of A(-11) and T(-7) in promoter melting and reveal important insights into the initiation of transcription bubble formation...
  8. Barany F, Danzitz M, Zebala J, Mayer A. Cloning and sequencing of genes encoding the TthHB8I restriction and modification enzymes: comparison with the isoschizomeric TaqI enzymes. Gene. 1992;112:3-12 pubmed
    ..However, codon usage and G+C content for the R-M genes differed markedly from that of other cloned Thermus genes. This suggests that these R-M genes were only recently introduced into the genus Thermus...
  9. Campbell E, Muzzin O, Chlenov M, Sun J, Olson C, Weinman O, et al. Structure of the bacterial RNA polymerase promoter specificity sigma subunit. Mol Cell. 2002;9:527-39 pubmed
    ..Positive control mutants in sigma(4) cluster in two regions, positioned to interact with activators bound just upstream or downstream of the -35 element. ..

More Information


  1. Zhang G, Campbell E, Minakhin L, Richter C, Severinov K, Darst S. Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 A resolution. Cell. 1999;98:811-24 pubmed
  2. Barany F, Slatko B, Danzitz M, Cowburn D, Schildkraut I, Wilson G. The corrected nucleotide sequences of the TaqI restriction and modification enzymes reveal a thirteen-codon overlap. Gene. 1992;112:91-5 pubmed
    ..Gene 112 (1992) 13-20]. Removal of the overlapping codons did not interfere with in vivo M.TaqI activity. We postulate the overlap plays a role in regulating taqIR expression. ..
  3. Murakami K, Masuda S, Campbell E, Muzzin O, Darst S. Structural basis of transcription initiation: an RNA polymerase holoenzyme-DNA complex. Science. 2002;296:1285-90 pubmed publisher
    ..The structure explains how holoenzyme recognizes promoters containing variably spaced -10 and -35 elements and provides the basis for models of the closed and open promoter complexes...
  4. Campbell E, Korzheva N, Mustaev A, Murakami K, Nair S, Goldfarb A, et al. Structural mechanism for rifampicin inhibition of bacterial rna polymerase. Cell. 2001;104:901-12 pubmed
    ..The structure, combined with biochemical results, explains the effects of Rif on RNAP function and indicates that the inhibitor acts by directly blocking the path of the elongating RNA when the transcript becomes 2 to 3 nt in length...
  5. Murakami K, Masuda S, Darst S. Crystallographic analysis of Thermus aquaticus RNA polymerase holoenzyme and a holoenzyme/promoter DNA complex. Methods Enzymol. 2003;370:42-53 pubmed
  6. Sundermeier T, Karzai A. Functional SmpB-ribosome interactions require tmRNA. J Biol Chem. 2007;282:34779-86 pubmed
    ..We propose that a 1:1:1 complex of SmpB.tmRNA.EF-Tu(GTP) recognizes and binds a stalled ribosome to initiate trans-translation. ..
  7. Cao W, Lu J, Barany F. Nucleotide sequences and gene organization of TaqI endonuclease isoschizomers from Thermus sp. SM32 and Thermus filiformis Tok6A1. Gene. 1997;197:205-14 pubmed
    ..Phylogenetic analysis suggests that initially TfiTok6A1I diverged from a common ancestor, then Tsp32IR branched out, and finally TaqI and TthHB8I diverged from each other during evolution...
  8. Wetmur J, Wong D, Ortiz B, Tong J, Reichert F, Gelfand D. Cloning, sequencing, and expression of RecA proteins from three distantly related thermophilic eubacteria. J Biol Chem. 1994;269:25928-35 pubmed