A mutational analysis of DNA mimicry by ocr, the gene 0.3 antirestriction protein of bacteriophage T7

Autor: Alan Cooper, Rachel Turkington, David T. F. Dryden, Margaret Nutley, Gareth A. Roberts, Emily H. Pritchard, Augoustinos S. Stephanou, Mark R. Tock

Publikováno v: Biochemical and Biophysical Research Communications. 378:129-132

The ocr protein of bacteriophage T7 is a structural and electrostatic mimic of approximately 24 base pairs of double-stranded B-form DNA. As such, it inhibits all Type I restriction and modification (R/M) enzymes by blocking their DNA binding grooves

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8d66f03ff4f506fe56dac614d015c32c
https://doi.org/10.1016/j.bbrc.2008.11.014

The CafA Protein Required for the 5′-Maturation of 16 S rRNA Is a 5′-End-dependent Ribonuclease That Has Context-dependent Broad Sequence Specificity

Autor: Mark R. Tock, Gregory Carroll, Kenneth J. McDowall, Andrew P. Walsh

Publikováno v: Journal of Biological Chemistry. 275:8726-8732

The CafA protein, which was initially described as having a role in either Escherichia coli cell division or chromosomal segregation, has recently been shown to be required for the maturation of the 5'-end of 16 S rRNA. The sequence of CafA is simila

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::257fe2c02c86651fd36abb5802638e77
https://doi.org/10.1074/jbc.275.12.8726

DNA bending by M.EcoKI methyltransferase is coupled to nucleotide flipping

Autor: Wilson C. K. Poon, David T. F. Dryden, Mark R. Tock, Stefan U. Egelhaaf, Tsueu-Ju Su

Publikováno v: Su, T-J, Tock, M R, Egelhaaf, S U, Poon, W C K & Dryden, D T F 2005, ' DNA bending by M.EcoKI methyltransferase is coupled to nucleotide flipping ', Nucleic Acids Research, vol. 33, no. 10, pp. 3235-3244 . https://doi.org/10.1093/nar/gki618
Nucleic Acids Research

The maintenance methyltransferase M.EcoKI recognizes the bipartite DNA sequence 5'-A (A) under bar CNNN-NNNG (T) under bar GC-3', where N is any nucleotide. M.EcoKI preferentially methylates a sequence already containing a methylated adenine at or co

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f913ae2388ba038eaba4c7d41755326c
https://hdl.handle.net/20.500.11820/589e3ab6-5985-4963-b5c0-80a05a880eba

Dynamic evidence for metal ion catalysis in the reaction mediated by a flap endonuclease

Autor: Mark R. Tock, Jane A. Grasby, Elaine Frary, Jon R. Sayers

Publikováno v: The EMBO journal. 22(5)

On the basis of structural work, metal ions are proposed to play a catalytic role in reactions mediated by many phosphoryl transfer enzymes. To gain dynamic support for such mechanisms, the role of metal ion cofactors in phosphate diester hydrolysis

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::26b05ec46dece1b35ef6620d38f6f9fe
https://pubmed.ncbi.nlm.nih.gov/12606565

Cleavage of poly(A) tails on the 3′-end of RNA by ribonuclease E of Escherichia coli

Autor: A von Gabain, Mark R. Tock, M. H. Mallen, Vladimir R. Kaberdin, Andrew P. Walsh, Kenneth J. McDowall

Publikováno v: Scopus-Elsevier

RNase E initiates the decay of Escherichia coli RNAs by cutting them internally near their 5′-end and is a component of the RNA degradosome complex, which also contains the 3′-exonuclease PNPase. Recently, RNase E has been shown to be able to rem

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d9e08ff0b20e66332580b7f18d9f6374
http://www.scopus.com/inward/record.url?eid=2-s2.0-0035339671&partnerID=MN8TOARS