Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Kate R. Lieberman"'
Publikováno v:
Biochemistry
Ribonucleoside triphosphates (rNTPs) are frequently incorporated during DNA synthesis by replicative DNA polymerases (DNAPs), and once incorporated are not efficiently edited by the DNAP exonucleolytic function. We examined the kinetic mechanisms tha
Publikováno v:
Journal of the American Chemical Society
Exonucleolytic editing of incorrectly incorporated nucleotides by replicative DNA polymerases (DNAPs) plays an essential role in the fidelity of DNA replication. Editing requires that the primer strand of the DNA substrate be transferred between the
Publikováno v:
Journal of Biological Chemistry. 289:6350-6361
The Φ29 DNA polymerase (DNAP) is a processive B-family replicative DNAP. Fluctuations between the pre-translocation and post-translocation states can be quantified from ionic current traces, when individual Φ29 DNAP-DNA complexes are held atop a na
Publikováno v:
Journal of the American Chemical Society. 135:9149-9155
Complexes formed between phi29 DNA polymerase (DNAP) and DNA fluctuate discretely between the pre-translocation and post-translocation states on the millisecond time scale. The translocation fluctuations can be observed in ionic current traces when i
Publikováno v:
Journal of the American Chemical Society. 134:18816-18823
Complexes formed between the bacteriophage phi29 DNA polymerase (DNAP) and DNA fluctuate between the pre-translocation and post-translocation states on the millisecond time scale. These fluctuations can be directly observed with single-nucleotide pre
Replicative DNA polymerases (DNAPs) require divalent metal cations for phosphodiester bond formation in the polymerase site and for hydrolytic editing in the exonuclease site. Me(2+) ions are intimate architectural components of each active site, whe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::00b7343e7c9ae54e23b4dc6daf8cb543
https://europepmc.org/articles/PMC4813572/
https://europepmc.org/articles/PMC4813572/
Autor:
Andre Marziali, Ai H. Mai, Hongyun Wang, Mark Akeson, Nahid N. Jetha, Joseph M. Dahl, Gerald M. Cherf, Kate R. Lieberman, Daniel R. Garalde
Publikováno v:
Journal of Biological Chemistry. 287:13407-13421
Complexes of phi29 DNA polymerase and DNA fluctuate on the millisecond time scale between two ionic current amplitude states when captured atop the α-hemolysin nanopore in an applied field. The lower amplitude state is stabilized by complementary dN
Autor:
Gerald M. Cherf, Joseph M. Dahl, Felix Olasagasti, Seico Benner, Mark Akeson, Kate R. Lieberman, David W. Deamer
Publikováno v:
Nature nanotechnology
Nanopores can be used to analyse DNA by monitoring ion currents as individual strands are captured and driven through the pore in single file by an applied voltage. Here, we show that serial replication of individual DNA templates can be achieved by
Autor:
Thomas Earnest, Rachel Green, Harry F. Noller, Raymond R. Samaha, Kate R. Lieberman, Jamie H. D. Cate, Kevin S. Wilson, Gulnara Yusupova, Simpson Joseph, Uwe von Ahsen, Lisa F. Newcomb, Gloria M. Culver, Marat Yusupov, Laura Lancaster, Lovisa Holmberg, Chuck Merryman, Anne Dallas
The study of the process of protein synthesis, which encompasses translation of the genetic code, has been intensively under way for about 4 decades. This chapter summarizes recent studies of the structure and function of ribosomes by a combination o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2cdde6fc3989b15ab29ede42034c1eef
https://doi.org/10.1128/9781555818142.ch13
https://doi.org/10.1128/9781555818142.ch13
Autor:
Mark A. Bayfield, Rachel Green, Daniel F. Kim, Steven T. Gregory, Albert E. Dahlberg, Kate R. Lieberman, Jill Thompson, Harry F. Noller, Michael O'Connor
Publikováno v:
Proceedings of the National Academy of Sciences. 98:9002-9007
On the basis of the recent atomic-resolution x-ray structure of the 50S ribosomal subunit, residues A2451 and G2447 of 23S rRNA were proposed to participate directly in ribosome-catalyzed peptide bond formation. We have examined the peptidyltransfera