Aminoacyl-tRNA synthetase genes of Bacillus subtilis: organization and regulation

1999 ◽  
Vol 77 (4) ◽  
pp. 343-347 ◽  
Author(s):  
Martin Pelchat ◽  
Jacques Lapointe
Keyword(s):  
Bacillus Subtilis ◽  
Initiation Site ◽  
Trna Synthetase ◽  
Translation Initiation Site ◽  
Aminoacyl Trna Synthetase ◽  
Gene Encoding ◽  
T Box ◽  
Trna Synthetases ◽  
Genes Encoding ◽  
Mature Mrnas

In Bacillus subtilis, 14 of the 24 genes encoding aminoacyl-tRNA synthetases (aaRS) are regulated by tRNA-mediated antitermination in response to starvation for their cognate aminoacid. Their transcripts have an untranslated leader mRNA of about 300 nucleotides, including alternative and mutually exclusive terminator-antiterminator structures, just upstream from the translation initiation site. Following antitermination, some of these transcripts are cleaved leaving at the 5prime-end of the mature mRNAs, stable secondary structures that can protect them against degradation. Although most B. subtilis aaRS genes are expressed as monocistronic mRNAs, the gltX gene encoding the glutamyl-tRNA synthetase is cotranscribed with cysE and cysS encoding serine acetyl-transferase and cysteinyl-tRNA synthetase, respectively. Transcription of gltX is not controlled by a tRNA, but tRNACys-mediated antitermination regulates the elongation of transcription into cysE and cysS. The full-length gltX-cysE-cysS transcript is then cleaved into a monocistronic gltX mRNA and a cysE-cysS mRNA.Key words: regulation, aminoacyl-tRNA synthetase, T-Box, processing.

scholarly journals The Bacillus subtilis tyrZ Gene Encodes a Highly Selective Tyrosyl-tRNA Synthetase and Is Regulated by a MarR Regulator and T Box Riboswitch

2015 ◽  
Vol 197 (9) ◽  
pp. 1624-1631 ◽  
Author(s):  
Rebecca N. Williams-Wagner ◽  
Frank J. Grundy ◽  
Medha Raina ◽  
Michael Ibba ◽  
Tina M. Henkin
Keyword(s):  
Bacillus Subtilis ◽  
Biofilm Formation ◽  
Normal Growth ◽  
Growth Conditions ◽  
Trna Synthetase ◽  
Cellular Proteins ◽  
Gene Encoding ◽  
Content Type ◽  
T Box ◽  
Related Compounds

ABSTRACTMisincorporation ofd-tyrosine (d-Tyr) into cellular proteins due to mischarging of tRNATyrwithd-Tyr by tyrosyl-tRNA synthetase inhibits growth and biofilm formation ofBacillus subtilis. Furthermore, manyB. subtilisstrains lack a functional gene encodingd-aminoacyl-tRNA deacylase, which prevents misincorporation ofd-Tyr in most organisms.B. subtilishas two genes that encode tyrosyl-tRNA synthetase:tyrSis expressed under normal growth conditions, andtyrZis known to be expressed only whentyrSis inactivated by mutation. We hypothesized thattyrZencodes an alternate tyrosyl-tRNA synthetase, expression of which allows the cell to grow whend-Tyr is present. We show that TyrZ is more selective forl-Tyr overd-Tyr than is TyrS; however, TyrZ is less efficient overall. We also show that expression oftyrZis required for growth and biofilm formation in the presence ofd-Tyr. BothtyrSandtyrZare preceded by a T box riboswitch, buttyrZis found in an operon withywaE, which is predicted to encode a MarR family transcriptional regulator. Expression oftyrZis repressed by YwaE and also is regulated at the level of transcription attenuation by the T box riboswitch. We conclude that expression oftyrZmay allow growth when excessd-Tyr is present.IMPORTANCEAccurate protein synthesis requires correct aminoacylation of each tRNA with the cognate amino acid and discrimination against related compounds.Bacillus subtilisproducesd-Tyr, an analog ofl-Tyr that is toxic when incorporated into protein, during stationary phase. Most organisms utilize ad-aminoacyl-tRNA deacylase to prevent misincorporation ofd-Tyr. This work demonstrates that the increased selectivity of the TyrZ form of tyrosyl-tRNA synthetase may provide a mechanism by whichB. subtilisprevents misincorporation ofd-Tyr in the absence of a functionald-aminoacyl-tRNA deacylase gene.

scholarly journals Characterization of an Inducible, Antibiotic-Resistant Aminoacyl-tRNA Synthetase Gene in Streptomyces coelicolor

2008 ◽  
Vol 190 (18) ◽  
pp. 6253-6257 ◽  
Author(s):  
James J. Vecchione ◽  
Jason K. Sello
Keyword(s):  
Streptomyces Coelicolor ◽  
Trna Synthetase ◽  
Aminoacyl Trna Synthetase ◽  
Antibiotic Resistant ◽  
Trna Synthetases ◽  
Genes Encoding

ABSTRACT Streptomyces coelicolor has two genes encoding tryptophanyl-tRNA synthetases, one of which (trpRS1) is resistant to and transcriptionally activated by indolmycin. We found that this gene also confers resistance to chuangxinmycin (another antibiotic that inhibits bacterial tryptophanyl-tRNA synthetases) and that its transcription is not absolutely dependent on either antibiotic.

A gene encoding a tyrosine tRNA synthetase is located near Sacs in Bacillus subtilis

DNA Sequence ◽  
1991 ◽  
Vol 1 (4) ◽  
pp. 251-261 ◽  
Author(s):  
P. Glaser ◽  
F. Kunst ◽  
M. Débarbouillé ◽  
A. Vertès ◽  
A. Danchin ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Trna Synthetase ◽  
Gene Encoding

scholarly journals Influence of Antisynthetase Antibodies Specificities on Antisynthetase Syndrome Clinical Spectrum Time Course

2019 ◽  
Vol 8 (11) ◽  
pp. 2013 ◽  
Author(s):  
Cavagna ◽  
Trallero-Araguás ◽  
Meloni ◽  
Cavazzana ◽  
Rojas-Serrano ◽  
...  
Keyword(s):  
Time Course ◽  
Clinical Presentation ◽  
Reference Group ◽  
Trna Synthetase ◽  
Antisynthetase Syndrome ◽  
Aminoacyl Trna Synthetase ◽  
Trna Synthetases ◽  
Aminoacyl Trna Synthetases ◽  
Antisynthetase Antibodies ◽  
Clinical Triad

Antisynthetase syndrome (ASSD) is a rare clinical condition that is characterized by the occurrence of a classic clinical triad, encompassing myositis, arthritis, and interstitial lung disease (ILD), along with specific autoantibodies that are addressed to different aminoacyl tRNA synthetases (ARS). Until now, it has been unknown whether the presence of a different ARS might affect the clinical presentation, evolution, and outcome of ASSD. In this study, we retrospectively recorded the time of onset, characteristics, clustering of triad findings, and survival of 828 ASSD patients (593 anti-Jo1, 95 anti-PL7, 84 anti-PL12, 38 anti-EJ, and 18 anti-OJ), referring to AENEAS (American and European NEtwork of Antisynthetase Syndrome) collaborative group’s cohort. Comparisons were performed first between all ARS cases and then, in the case of significance, while using anti-Jo1 positive patients as the reference group. The characteristics of triad findings were similar and the onset mainly began with a single triad finding in all groups despite some differences in overall prevalence. The “ex-novo” occurrence of triad findings was only reduced in the anti-PL12-positive cohort, however, it occurred in a clinically relevant percentage of patients (30%). Moreover, survival was not influenced by the underlying anti-aminoacyl tRNA synthetase antibodies’ positivity, which confirmed that antisynthetase syndrome is a heterogeneous condition and that antibody specificity only partially influences the clinical presentation and evolution of this condition.

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 The Staphylococcus aureus ileS gene, encoding isoleucyl-tRNA synthetase, is a member of the T-box family.

1997 ◽  
Vol 179 (11) ◽  
pp. 3767-3772 ◽  
Author(s):  
F J Grundy ◽  
M T Haldeman ◽  
G M Hornblow ◽  
J M Ward ◽  
A F Chalker ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Trna Synthetase ◽  
Gene Encoding ◽  
T Box

scholarly journals The Evolutionary Fate of Mitochondrial Aminoacyl-tRNA Synthetases in Amitochondrial Organisms

2021 ◽  
Author(s):  
Gabor L. Igloi
Keyword(s):  
Protein Sequence ◽  
Identity Element ◽  
Mitochondrial Gene ◽  
Trna Synthetase ◽  
Aminoacyl Trna Synthetase ◽  
Trna Synthetases ◽  
Aminoacyl Trna Synthetases ◽  
Cognate Trna ◽  
Evolutionary Fate ◽  
Endosymbiotic Evolution

AbstractDuring the endosymbiotic evolution of mitochondria, the genes for aminoacyl-tRNA synthetases were transferred to the ancestral nucleus. A further reduction of mitochondrial function resulted in mitochondrion-related organisms (MRO) with a loss of the organelle genome. The fate of the now redundant ancestral mitochondrial aminoacyl-tRNA synthetase genes is uncertain. The derived protein sequence for arginyl-tRNA synthetase from thirty mitosomal organisms have been classified as originating from the ancestral nuclear or mitochondrial gene and compared to the identity element at position 20 of the cognate tRNA that distinguishes the two enzyme forms. The evolutionary choice between loss and retention of the ancestral mitochondrial gene for arginyl-tRNA synthetase reflects the coevolution of arginyl-tRNA synthetase and tRNA identity elements.

scholarly journals The Escherichia coli serS gene promoter region overlaps with the rarA gene

2021 ◽  
Author(s):  
Kanika Jain ◽  
Tyler H. Stanage ◽  
Elizabeth A. Wood ◽  
Michael M. Cox
Keyword(s):  
Escherichia Coli ◽  
Promoter Region ◽  
Gene Promoter ◽  
Stringent Response ◽  
Trna Synthetase ◽  
Growth Defect ◽  
Aminoacyl Trna Synthetase ◽  
Gene Encoding ◽  
Gene Promoter Region ◽  
Entire Gene

Deletion of the entire gene encoding the RarA protein of Escherichia coli results in a growth defect and additional deficiencies that were initially ascribed to a lack of RarA function. Further work revealed that most of the effects reflected the presence of sequences in the rarA gene that affect expression of the downstream gene, serS. The serS gene encodes the seryl aminoacyl-tRNA synthetase. Decreases in the expression of serS can trigger the stringent response. The sequences that affect serS expression are located in the last 15 nucleotides of the rarA gene.

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