Developmental regulation of the gene for formate dehydrogenase in Neurospora crassa

Chow, C M; RajBhandary, U L

doi:10.1128/jb.175.12.3703-3709.1993

Cited by 41 publications

(36 citation statements)

References 42 publications

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“…Finally, the most definitive indication that tRNA Tyr recognition differs between bacteria and humans comes from the observation that the B. stearothermophilus and human enzymes are unable to aminoacylate each other's tRNA Tyr substrates. These results are in good agreement with previously published comparisons between bacterial and eukaryotic tyrosyl-tRNA synthetases (17)(18)(19)(20)(21). Similar species specificity has also been observed for several other aminoacyl-tRNA synthetases (55)(56)(57)(58)(59) and is consistent with the hypothesis that the recognition of tRNA by aminoacyl-tRNA synthetases was still evolving after the divergence of bacteria and eukaryotes (39).…”

Section: Resultssupporting

confidence: 82%

“…Comparison of tRNA Tyr sequences indicates that in bacteria, tRNA Tyr is a type II tRNA, whereas in eukaryotes tRNA Tyr is a type I tRNA (16,17), supporting the above hypothesis. Comparison of the amino acid sequences of tyrosyl-tRNA synthetases further supports the above hypothesis.…”

Section: Resultssupporting

confidence: 66%

“…In this regard, tRNA Tyr is unique among tRNAs in that the nucleotide sequence of bacterial tRNA Tyr is a type II tRNA sequence, whereas eukaryotic tRNA Tyr sub- 6 M. Mirande, personal communication. strates are type I tRNAs (16,17). Differences in tRNA Tyr recognition should also be reflected in the amino acid sequences of bacterial and eukaryotic tyrosyl-tRNA synthetases.…”

Section: Resultsmentioning

confidence: 99%

“…Tyrosyl-tRNA (tRNA Tyr ) is unique among tRNAs in that in bacteria it is type II (which contains an extended variable loop), whereas in eukaryotes it is type I (16,17). Furthermore, previous studies indicate that bacterial and eukaryotic tyrosyl-tRNA synthetases do not catalyze the aminoacylation of other tRNA Tyr substrates suggesting that tRNA Tyr recognition differs between bacteria and eukaryotes (17)(18)(19)(20)(21). If this hypothesis is correct, it should be possible to exploit this species specificity to design novel antibiotics that selectively inhibit bacterial tyrosyl-tRNA synthetases.…”

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confidence: 99%

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Human Tyrosyl-tRNA Synthetase Shares Amino Acid Sequence Homology with a Putative Cytokine

Kleeman¹,

Wei²,

Simpson

et al. 1997

Journal of Biological Chemistry

116

102

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To test the hypothesis that tRNA Tyr recognition differs between bacterial and human tyrosyl-tRNA synthetases, we sequenced several clones identified as human tyrosyl-tRNA synthetase cDNAs by the Human Genome Project. We found that human tyrosyl-tRNA synthetase is composed of three domains: 1) an aminoterminal Rossmann fold domain that is responsible for formation of the activated E⅐Tyr-AMP intermediate and is conserved among bacteria, archeae, and eukaryotes; 2) a tRNA anticodon recognition domain that has not been conserved between bacteria and eukaryotes; and 3) a carboxyl-terminal domain that is unique to the human tyrosyl-tRNA synthetase and whose primary structure is 49% identical to the putative human cytokine endothelial monocyte-activating protein II, 50% identical to the carboxyl-terminal domain of methionyl-tRNA synthetase from Caenorhabditis elegans, and 43% identical to the carboxyl-terminal domain of Arc1p from Saccharomyces cerevisiae. The first two domains of the human tyrosyl-tRNA synthetase are 52, 36, and 16% identical to tyrosyl-tRNA synthetases from S. cerevisiae, Methanococcus jannaschii, and Bacillus stearothermophilus, respectively. Nine of fifteen amino acids known to be involved in the formation of the tyrosyl-adenylate complex in B. stearothermophilus are conserved across all of the organisms, whereas amino acids involved in the recognition of tRNA Tyr are not conserved. Kinetic analyses of recombinant human and B. stearothermophilus tyrosyl-tRNA synthetases expressed in Escherichia coli indicate that human tyrosyl-tRNA synthetase aminoacylates human but not B. stearothermophilus tRNA Tyr , and vice versa, supporting the original hypothesis. It is proposed that like endothelial monocyte-activating protein II and the carboxyl-terminal domain of Arc1p, the carboxyl-terminal domain of human tyrosyltRNA synthetase evolved from gene duplication of the carboxyl-terminal domain of methionyl-tRNA synthetase and may direct tRNA to the active site of the enzyme.Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. For most aminoacyl-tRNA synthetases (E), tRNA aminoacylation can be separated into two steps: formation of a stable enzyme-bound aminoacyladenylate intermediate (E⅐AA-AMP, Equation 1), followed by transfer of the amino acid (AA) from the aminoacyl-adenylate intermediate to the 3Ј end of the tRNA substrate (Equation 2).The 20 different aminoacyl-tRNA synthetases fall into two distinct structural classes (1, 2). Class I aminoacyl-tRNA synthetases (of which tyrosyl-tRNA synthetase is a member) are characterized by a structurally well conserved amino-terminal Rossmann fold domain which contains the signature sequences "HIGH" and "KMSKS" (3, 4). In contrast, the carboxyl-terminal domains of class I aminoacyl-tRNA synthetases are structurally diverse suggesting that the primordial aminoacyl-tRNA synthetase consisted solely of the amino-terminal Rossmann fold (5-8). Both x-ray crystallography and site-directed mutagenesis of class I aminoacyl-tRNA synthet...

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Section: Resultssupporting

confidence: 82%

Section: Resultssupporting

confidence: 66%

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

See 2 more Smart Citations

Human Tyrosyl-tRNA Synthetase Shares Amino Acid Sequence Homology with a Putative Cytokine

Kleeman¹,

Wei²,

Simpson

et al. 1997

Journal of Biological Chemistry

116

102

View full text Add to dashboard Cite

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“…Plasmids. The plasmids pETTyrRS, pACamG, and pRSVCATam27 carrying the U2:A71͞U35A36͞G72 mutant tRNA 2 fMet gene have been described previously (19). E. coli UQ27 containing the plasmid pUCProRS was obtained from W. McClain (Univ.…”

Section: Methodsmentioning

confidence: 99%

Twenty-first aminoacyl-tRNA synthetase–suppressor tRNA pairs for possible use in site-specific incorporation of amino acid analogues into proteins in eukaryotes and in eubacteria

Kowal

Köhrer

RajBhandary

2001

Proc. Natl. Acad. Sci. U.S.A.

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Two critical requirements for developing methods for the sitespecific incorporation of amino acid analogues into proteins in vivo are (i) a suppressor tRNA that is not aminoacylated by any of the endogenous aminoacyl-tRNA synthetases (aaRSs) and (ii) an aminoacyl-tRNA synthetase that aminoacylates the suppressor tRNA but no other tRNA in the cell. Here we describe two such aaRSsuppressor tRNA pairs, one for use in the yeast Saccharomyces cerevisiae and another for use in Escherichia coli. The "21st synthetase-tRNA pairs" include E. coli glutaminyl-tRNA synthetase (GlnRS) along with an amber suppressor derived from human initiator tRNA, for use in yeast, and mutants of the yeast tyrosyltRNA synthetase (TyrRS) along with an amber suppressor derived from E. coli initiator tRNA, for use in E. coli. The suppressor tRNAs are aminoacylated in vivo only in the presence of the heterologous aaRSs, and the aminoacylated tRNAs function efficiently in suppression of amber codons. Plasmids carrying the E. coli GlnRS gene can be stably maintained in yeast. However, plasmids carrying the yeast TyrRS gene could not be stably maintained in E. coli. This lack of stability is most likely due to the fact that the wild-type yeast TyrRS misaminoacylates the E. coli proline tRNA. By using errorprone PCR, we have isolated and characterized three mutants of yeast TyrRS, which can be stably expressed in E. coli. These mutants still aminoacylate the suppressor tRNA essentially quantitatively in vivo but show increased discrimination in vitro for the suppressor tRNA over the E. coli proline tRNA by factors of 2.2-to 6.8-fold.

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Functional genomic profiling of Aspergillus fumigatus biofilm reveals enhanced production of the mycotoxin gliotoxin

et al. 2010

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The opportunistic pathogenic mold Aspergillus fumigatus is an increasing cause of morbidity and mortality in immunocompromised and in part immunocompetent patients. A. fumigatus can grow in multicellular communities by the formation of a hyphal network encased in an extracellular matrix. Here, we describe the proteome and transcriptome of planktonic- and biofilm-grown A. fumigatus mycelium after 24 and 48 h. A biofilm- and time-dependent regulation of many proteins and genes of the primary metabolism indicates a developmental stage of the young biofilm at 24 h, which demands energy. At a matured biofilm phase, metabolic activity seems to be reduced. However, genes, which code for hydrophobins, and proteins involved in the biosynthesis of secondary metabolites were significantly upregulated. In particular, proteins of the gliotoxin secondary metabolite gene cluster were induced in biofilm cultures. This was confirmed by real-time PCR and by detection of this immunologically active mycotoxin in culture supernatants using HPLC analysis. The enhanced production of gliotoxin by in vitro formed biofilms reported here may also play a significant role under in vivo conditions. It may confer A. fumigatus protection from the host immune system and also enable its survival and persistence in chronic lung infections such as aspergilloma.

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Developmental regulation of the gene for formate dehydrogenase in Neurospora crassa

Cited by 41 publications

References 42 publications

Human Tyrosyl-tRNA Synthetase Shares Amino Acid Sequence Homology with a Putative Cytokine

Human Tyrosyl-tRNA Synthetase Shares Amino Acid Sequence Homology with a Putative Cytokine

Twenty-first aminoacyl-tRNA synthetase–suppressor tRNA pairs for possible use in site-specific incorporation of amino acid analogues into proteins in eukaryotes and in eubacteria

Functional genomic profiling of Aspergillus fumigatus biofilm reveals enhanced production of the mycotoxin gliotoxin

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