Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Heather C. O′Farrell"'
Autor:
Jason P. Rife, Lei Wang, Gordon L. Archer, Heather C. O'Farrell, Martin K. Safo, Sam Boundy, Faik N. Musayev
Publikováno v:
Journal of Biological Chemistry. 288:132-140
The gene orfX is conserved among all staphylococci, and its complete sequence is maintained upon insertion of the staphylococcal chromosome cassette mec (SCCmec) genomic island, containing the gene encoding resistance to β-lactam antibiotics (mecA),
Autor:
Zhili Xu, Leah A. Pogorzala, Faik N. Musayev, Nagesh Pulicherla, Gloria M. Culver, Jason P. Rife, Heather C. O′Farrell, J. Neel Scarsdale, Elaine A. Sia
Publikováno v:
Journal of Molecular Biology. 391:884-893
The enzymes of the KsgA/Dim1 family are universally distributed throughout all phylogeny; however, structural and functional differences are known to exist. The well-characterized function of these enzymes is to dimethylate two adjacent adenosines of
Publikováno v:
RNA. 12:725-733
Ribosome biogenesis is a complicated process, involving numerous cleavage, base modification and assembly steps. All ribosomes share the same general architecture, with small and large subunits made up of roughly similar rRNA species and a variety of
Publikováno v:
Journal of Biological Chemistry
The Journal of biological chemistry
The Journal of biological chemistry
The assembly of the ribosomal subunits is facilitated by ribosome biogenesis factors. The universally conserved methyltransferase KsgA modifies two adjacent adenosine residues in the 3'-terminal helix 45 of the 16 S ribosomal RNA (rRNA). KsgA recogni
Publikováno v:
Biochemistry. 51(1)
The KsgA methyltransferase is universally conserved and plays a key role in regulating ribosome biogenesis. KsgA has a complex reaction mechanism, transferring a total of four methyl groups onto two separate adenosine residues, A1518 and A1519, in th
Publikováno v:
Biochemistry. 49(12)
The KsgA/Dim1 family of proteins is intimately involved in ribosome biogenesis in all organisms. These enzymes share the common function of dimethylating two adenosine residues near the 3'-OH end of the small subunit rRNA; orthologs in the three king
Publikováno v:
Nature structuralmolecular biology. 15(5)
In contrast to the diversity of most ribosomal RNA modification patterns and systems, the KsgA methyltransferase family seems to be nearly universally conserved along with the modifications it catalyzes. Our data reveal that KsgA interacts with small
Publikováno v:
Journal of molecular biology. 339(2)
The bacterial enzyme KsgA catalyzes the transfer of a total of four methyl groups from S-adenosyl- l -methionine (S-AdoMet) to two adjacent adenosine bases in 16 S rRNA. This enzyme and the resulting modified adenosine bases appear to be conserved in
Autor:
Jason P. Rife, Heather C. O'Farrell
Publikováno v:
BMC Microbiology, Vol 12, Iss 1, p 244 (2012)
BMC Microbiology
BMC Microbiology
Background The KsgA methyltransferase has been conserved throughout evolution, methylating two adenosines in the small subunit rRNA in all three domains of life as well as in eukaryotic organelles that contain ribosomes. Understanding of KsgA’s imp
Publikováno v:
BMC Research Notes
BMC Research Notes, Vol 1, Iss 1, p 108 (2008)
BMC Research Notes, Vol 1, Iss 1, p 108 (2008)
Background One of the 60 or so genes conserved in all domains of life is the ksgA/dim1 orthologous group. Enzymes from this family perform the same post-transcriptional nucleotide modification in ribosome biogenesis, irrespective of organism. Despite