scholarly journals Arginyl-tRNA synthetase with signature sequence KMSK from Bacillus stearothermophilus

2003 ◽  
Vol 376 (3) ◽  
pp. 773-779 ◽  
Author(s):  
Juan LI ◽  
Yong-Neng YAO ◽  
Mo-Fang LIU ◽  
En-Duo WANG
Keyword(s):  
Amino Acid ◽  
Bacillus Stearothermophilus ◽  
Genomic Sequence ◽  
Trna Synthetase ◽  
Class I ◽  
Acid Activation ◽  
Gene Encoding ◽  
Mutual Compensation ◽  
Nickel Affinity Chromatography ◽  
High Loop

ArgRS (arginyl-tRNA synthetase) belongs to the class I aaRSs (aminoacyl-tRNA synthetases), though the majority of ArgRS species lack the canonical KMSK sequence characteristic of class I aaRSs. A DNA fragment of the ArgRS gene from Bacillus stearothermophilus was amplified using primers designed according to the conserved regions of known ArgRSs. Through analysis of the amplified DNA sequence and known tRNAArgs with a published genomic sequence of B. stearothermophilus, the gene encoding ArgRS (argS´) was amplified by PCR and the gene encoding tRNAArg (ACG) was synthesized. ArgRS contained 557 amino acid residues including the canonical KMKS sequence. Recombinant ArgRS and tRNAArg (ACG) were expressed in Escherichia coli. ArgRS purified by nickel-affinity chromatography had no ATPase activity. The kinetics of ArgRS and cross-recognition between ArgRSs and tRNAArgs from B. stearothermophilus and E. coli were studied. The activities of B. stearothermophilus ArgRS mutated at Lys382 and Lys385 of the KMSK sequence and at Gly136 upstream of the HIGH loop were determined. From the mutation results, we concluded that there was mutual compensation of Lys385 and Gly136 for the amino acid-activation activity of B. stearothermophilus ArgRS.

scholarly journals Characterization of Gmhsp26-A, a stress gene encoding a divergent heat shock protein of soybean: heavy-metal-induced inhibition of intron processing.

1988 ◽  
Vol 8 (3) ◽  
pp. 1113-1122 ◽  
Author(s):  
E Czarnecka ◽  
R T Nagao ◽  
J L Key ◽  
W B Gurley
Keyword(s):  
Amino Acid ◽  
Heat Shock ◽  
Amino Acid Sequence ◽  
Genomic Sequence ◽  
Stress Protein ◽  
Initiation Site ◽  
Gene Encoding ◽  
S1 Nuclease ◽  
Soybean Seedlings ◽  
Nuclease Mapping

We determined the DNA sequence and mapped the corresponding transcripts of a genomic clone containing the Gmhsp26-A gene of soybean. This gene is homologous to the previously characterized cDNA clone pCE54 (E. Czarnecka, L. Edelman, F. Schöffl, and J. L. Key, Plant Mol. Biol. 3:45-58, 1984) and is expressed in response to a wide variety of physiological stresses including heat shock (HS). S1 nuclease mapping of transcripts and a comparison of the cDNA sequence with the genomic sequence indicated the presence of a soybean seedlings with either CdCl2 or CuSO4. Analysis of the 5' termini of transcripts indicated the presence of one major and at least two minor start sites. In each case, initiation occurred 27 to 30 base pairs downstream from a TATA-like motif, and thus each initiation site appears to be promoted by the activity of a separate subpromoter. The three subpromoters are all associated with sequences showing low homology to the HS consensus element of Drosophila melanogaster HS genes and are differentially induced in response to various stresses. Within the carboxyl-terminal half of the protein, hydropathy analysis of the deduced amino acid sequence indicated a high degree of relatedness to the small HS proteins. A comparison of the primary amino acid sequence of hsp26-A with sequences of the small HS proteins suggested that this stress protein is highly diverged and may therefore be specialized for stress adaptation in soybean.

Nucleotide Determinants for tRNA-Dependent Amino Acid Discrimination by a Class I tRNA Synthetase†

Biochemistry ◽  
1999 ◽  
Vol 38 (51) ◽  
pp. 16898-16903 ◽  
Author(s):  
Mark A. Farrow ◽  
Brian E. Nordin ◽  
Paul Schimmel
Keyword(s):  
Amino Acid ◽  
Trna Synthetase ◽  
Class I

Characterization of Gmhsp26-A, a stress gene encoding a divergent heat shock protein of soybean: heavy-metal-induced inhibition of intron processing

1988 ◽  
Vol 8 (3) ◽  
pp. 1113-1122
Author(s):  
E Czarnecka ◽  
R T Nagao ◽  
J L Key ◽  
W B Gurley
Keyword(s):  
Amino Acid ◽  
Heat Shock ◽  
Amino Acid Sequence ◽  
Genomic Sequence ◽  
Stress Protein ◽  
Initiation Site ◽  
Gene Encoding ◽  
S1 Nuclease ◽  
Soybean Seedlings ◽  
Nuclease Mapping

We determined the DNA sequence and mapped the corresponding transcripts of a genomic clone containing the Gmhsp26-A gene of soybean. This gene is homologous to the previously characterized cDNA clone pCE54 (E. Czarnecka, L. Edelman, F. Schöffl, and J. L. Key, Plant Mol. Biol. 3:45-58, 1984) and is expressed in response to a wide variety of physiological stresses including heat shock (HS). S1 nuclease mapping of transcripts and a comparison of the cDNA sequence with the genomic sequence indicated the presence of a soybean seedlings with either CdCl2 or CuSO4. Analysis of the 5' termini of transcripts indicated the presence of one major and at least two minor start sites. In each case, initiation occurred 27 to 30 base pairs downstream from a TATA-like motif, and thus each initiation site appears to be promoted by the activity of a separate subpromoter. The three subpromoters are all associated with sequences showing low homology to the HS consensus element of Drosophila melanogaster HS genes and are differentially induced in response to various stresses. Within the carboxyl-terminal half of the protein, hydropathy analysis of the deduced amino acid sequence indicated a high degree of relatedness to the small HS proteins. A comparison of the primary amino acid sequence of hsp26-A with sequences of the small HS proteins suggested that this stress protein is highly diverged and may therefore be specialized for stress adaptation in soybean.

The Human EPRS Locus (Formerly the QARS Locus): A Gene Encoding a Class I and a Class II Aminoacyl-tRNA Synthetase

Genomics ◽  
1994 ◽  
Vol 19 (2) ◽  
pp. 280-290 ◽  
Author(s):  
Eva Kaiser ◽  
Bing Hu ◽  
Stefanie Becher ◽  
Dirk Eberhard ◽  
Beate Schray ◽  
...  
Keyword(s):  
Class Ii ◽  
Trna Synthetase ◽  
Class I ◽  
Aminoacyl Trna Synthetase ◽  
Gene Encoding

scholarly journals Amino Acid-dependent Transfer RNA Affinity in a Class I Aminoacyl-tRNA Synthetase

2005 ◽  
Vol 280 (25) ◽  
pp. 23966-23977 ◽  
Author(s):  
Nathan T. Uter ◽  
Ita Gruic-Sovulj ◽  
John J. Perona
Keyword(s):  
Amino Acid ◽  
Trna Synthetase ◽  
Transfer Rna ◽  
Class I ◽  
Aminoacyl Trna Synthetase

Amino Acid Discrimination by a Class I Aminoacyl-tRNA Synthetase Specified by Negative Determinants

2003 ◽  
Vol 328 (2) ◽  
pp. 395-408 ◽  
Author(s):  
Timothy L. Bullock ◽  
Nathan Uter ◽  
T. Amar Nissan ◽  
John J. Perona
Keyword(s):  
Amino Acid ◽  
Trna Synthetase ◽  
Class I ◽  
Aminoacyl Trna Synthetase
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