Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Richard S. A. Lipman"'
Publikováno v:
Biochemistry. 42:7487-7496
Aminoacyl-tRNA synthetases are essential enzymes that catalyze attachment of amino acids to tRNAs for decoding of genetic information. In higher eukaryotes, several synthetases associate with non-synthetase proteins to form a high-molecular mass comp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ee45ce32962dd2b01a3ba2db64dce3f0
https://doi.org/10.1021/bi0344533
https://doi.org/10.1021/bi0344533
Publikováno v:
Journal of Molecular Biology. 315:943-949
Accurate aminoacylation of tRNAs by aminoacyl-tRNA synthetase is essential for the fidelity of protein synthesis. For Methanococcus jannaschii tRNA Pro , accuracy is difficult because the cognate prolyl-tRNA synthetase also recognizes and aminoacylat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::68d7ee19c712cc36ed82b5d9fb844264
https://doi.org/10.1006/jmbi.2001.5297
https://doi.org/10.1006/jmbi.2001.5297
Publikováno v:
Journal of Molecular Biology. 303:503-514
The core of Escherichia coli tRNA Cys is important for aminoacylation of the tRNA by cysteine-tRNA synthetase. This core differs from the common tRNA core by having a G15:G48, rather than a G15:C48 base-pair. Substitution of G15:G48 with G15:C48 decr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ef50657f13cc8c2b2d4dfcf08e830621
https://doi.org/10.1006/jmbi.2000.4169
https://doi.org/10.1006/jmbi.2000.4169
Publikováno v:
Biochemistry. 39:7792-7798
Synthesis of cysteinyl-tRNA(Cys) by cysteine-tRNA synthetase is required for decoding cysteine codons in all known organisms. The genome of the archaeon Methanococcus jannaschii lacks the gene for a normal cysteine-tRNA synthetase. The activity of th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0da5cda49ed6335e231cc1dd6d3849e9
https://doi.org/10.1021/bi0004955
https://doi.org/10.1021/bi0004955
Autor:
Richard S. A. Lipman, Brian S. Sproat, Kate Juliet Newberry, Timothy L. Bullock, Barbro Beijer, Ya-Ming Hou, Luke D. Sherlin, John J. Perona
Publikováno v:
Journal of Molecular Biology. 299:431-446
The position of the tertiary Levitt pair between nucleotides 15 and 48 in the transfer RNA core region suggests a key role in stabilizing the joining of the two helical domains, and in maintaining the relative orientations of the D and variable loops
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3d4cfca0068d7de3b521e8191f52472f
https://doi.org/10.1006/jmbi.2000.3749
https://doi.org/10.1006/jmbi.2000.3749
Publikováno v:
Biochemistry. 39:6791-6798
The conformation of a tRNA in its initial contact with its cognate aminoacyl-tRNA synthetase was investigated with the Escherichia coli glutamyl-tRNA synthetase-tRNA(Glu) complex. Covalent complexes between the periodate-oxidized tRNA(Glu) and its sy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3b85fda8089d723ca8c50360abc200aa
https://doi.org/10.1021/bi992477x
https://doi.org/10.1021/bi992477x
Publikováno v:
Scopus-Elsevier
The core region of Escherichia coli tRNA(Cys)is important for aminoacylation of the tRNA. This core contains an unusual G15:G48 base pair, and three adenosine nucleotides A13, A22 and A46 that are likely to form a 46:[13:22] adenosine base triple. We
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9ec1d7154366eab01bc14abd877d456b
https://doi.org/10.1093/nar/27.24.4743
https://doi.org/10.1093/nar/27.24.4743
Publikováno v:
Journal of Bacteriology. 181:5880-5884
The complete genomic sequencing of Methanococcus jannaschii cannot identify the gene for the cysteine-specific member of aminoacyl-tRNA synthetases. However, we show here that enzyme activity is present in the cell lysate of M. jannaschii . The demon
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bf6db89b48fd835b067220151722cdd9
https://doi.org/10.1128/jb.181.18.5880-5884.1999
https://doi.org/10.1128/jb.181.18.5880-5884.1999
Publikováno v:
RNA. 4:733-738
The CCA end is common to all tRNAs as the universal site for amino acid attachment+ It is also conserved in the 39-terminal tRNA-like structure of viral genomes that can be aminoacylated by an aminoacyl-tRNA synthetase (Florentz & Giege, 1995)+ Durin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4edeb5c7329c0fbb293b382c4c5bfe6a
https://doi.org/10.1017/s1355838298980281
https://doi.org/10.1017/s1355838298980281
Publikováno v:
Biochemistry. 35:7968-7973
The folate chromophore in native Escherichia coli DNA photolyase ([6R]-5,10-CH+-H4Pte(Glu)n=3-6) serves as an antenna, transferring light energy to the fully reduced flavin (FADH2) reaction center at high efficiency (EET = 0.92). Apophotolyase recons
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::899c8996a3f368bb31305e5f0906a1a3
https://doi.org/10.1021/bi9605548
https://doi.org/10.1021/bi9605548