Zobrazeno 1 - 10
of 211
pro vyhledávání: '"Ira G. Wool"'
Autor:
Yuen-Ling Chan, Ira G. Wool
Publikováno v:
Journal of Molecular Biology. 378:12-19
The elongation stage of protein synthesis consists of repeated cycles of the binding of aminoacyl-tRNA, peptide bond formation, and translocation. The process is normally catalyzed by the elongation factors Tu and G; however, the reactions can procee
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::deca2c33b8e10dd7b261fc4e76382c97
https://doi.org/10.1016/j.jmb.2008.02.016
https://doi.org/10.1016/j.jmb.2008.02.016
Publikováno v:
Journal of Biological Chemistry. 281:13478-13484
The nucleotides in domain I of 18 S rRNA that are important for the binding of the essential yeast ribosomal protein YS11 are mainly in a kink-turn motif and the terminal loop of helix 11 (H11). In the atomic structure of the Thermus thermophilus 30
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d94f9905a364fbe203431e836a6c3216
https://doi.org/10.1074/jbc.m513036200
https://doi.org/10.1074/jbc.m513036200
Publikováno v:
Journal of Molecular Biology. 355:1014-1025
There are a large number of tertiary contacts between nucleotides in 23 S rRNA, but which are of functional importance is not known. Disruption of one between A2662 in the sarcin/ricin loop (SRL) and A2531 in the peptidyl-transferase center (PTC) has
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fd12db1b298781d7af14fc18d5aa3601
https://doi.org/10.1016/j.jmb.2005.11.037
https://doi.org/10.1016/j.jmb.2005.11.037
Publikováno v:
Journal of Molecular Biology. 337:263-272
During translocation peptidyl-tRNA moves from the A-site to the P-site and mRNA is displaced by three nucleotides in the 3' direction. This reaction is catalyzed by elongation factor-G (EF-G) and is associated with ribosome-dependent hydrolysis of GT
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::63a428e21790f377baa4c71a04e84187
https://doi.org/10.1016/j.jmb.2004.01.020
https://doi.org/10.1016/j.jmb.2004.01.020
Autor:
Anton Glück, Ira G. Wool
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1594:115-126
A series of contiguous deletions were made in a cDNA encoding the ribonuclease restrictocin with the purpose of identifying the amino acids that are essential for the cleavage of the phosphodiester bond on the 3′ side of G4325 in the α-sarcin/rici
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f61dbd318f1cee2401de24c44aa2fec4
https://doi.org/10.1016/s0167-4838(01)00290-4
https://doi.org/10.1016/s0167-4838(01)00290-4
The sarcin-ricin domain (SRD) of Escherichia coli 23S rRNA, which includes a near-universal, purine rich sequence of 12 nucleotides, is the site of action of the eponymous ribotoxins. The chapter focuses on the structure of SRD. There is an evidence
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6f02679504814e724bca65d67d02bca2
https://doi.org/10.1128/9781555818142.ch38
https://doi.org/10.1128/9781555818142.ch38
Publikováno v:
Journal of Molecular Biology. 294:909-919
Eukaryotic ribosomes have a large number of proteins but the exact nature of their contribution to the structure and to the function of the particle is not known. Of the 78 proteins in yeast ribosomes, six have zinc finger motifs of the C2-C2 variety
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::82f56a584a14f15319d047777cf7b55e
https://doi.org/10.1006/jmbi.1999.3309
https://doi.org/10.1006/jmbi.1999.3309
Publikováno v:
Journal of Molecular Biology. 292:275-287
The sarcin/ricin domain of 23 S – 28 S ribosomal RNA is essential for protein synthesis because it forms a critical part of the binding site for elongation factors. A crystal structure of an RNA of 27 nucleotides that mimics the domain in Escherich
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::be72e0e0efe820d48feb1feb050dd276
https://doi.org/10.1006/jmbi.1999.3072
https://doi.org/10.1006/jmbi.1999.3072
Autor:
Mark R. Macbeth, Ira G. Wool
Publikováno v:
Journal of Molecular Biology. 285:567-580
The sarcin/ricin domain in 23 S/28 S rRNA is crucial for ribosome function, since it constitutes at least part of the binding site for the elongation factors and hence is essential for binding aminoacyl-tRNA and for translocation. The domain is also
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d3777a51136def3aa8a30a50e955818c
https://doi.org/10.1006/jmbi.1998.2337
https://doi.org/10.1006/jmbi.1998.2337
Autor:
Ira G. Wool, Mark R. Macbeth
Publikováno v:
Journal of Molecular Biology. 285:965-975
The sarcin/ricin domain (SRD) in Escherichia coli 23 S rRNA forms a part of the site for the association of the elongation factors with the ribosome and hence is critical for the binding of aminoacyl-tRNA and for translocation. The domain is also the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae93c6d2ca77ae6dc3ba002df75ef52c
https://doi.org/10.1006/jmbi.1998.2388
https://doi.org/10.1006/jmbi.1998.2388