The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
Gene Review

argS  -  arginyl-tRNA synthetase

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK1877, JW1865, lov
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of argS

  • Expression of the argS gene in B. lactofermentum and E. coli resulted in an increase in aminoacyl-tRNA synthetase activity, correlated with the presence in sodium dodecyl sulfate-polyacrylamide gels of a clear protein band that corresponds to this enzyme [1].
  • The Brevibacterium lactofermentum argS gene, which encodes an arginyl-tRNA synthetase, was identified in the upstream region of the lysA gene [1].
 

High impact information on argS

 

Chemical compound and disease context of argS

 

Anatomical context of argS

  • The allele specificity of the suppression suggests that the lov gene product may interact directly with the ribosomes [2].
 

Associations of argS with chemical compounds

  • The lov gene product thus seems to define a link between PBP2 (the mecillinam target) and the ribosomes; we propose that this link is involved in transmitting information on the growth rate (ribosome concentration) to the peptidoglycan synthesizing apparatus [2].
  • This finding emphasizes the necessity of using pure arginyl-tRNA synthetase in order to study the possible regulatory involvement of this enzyme in the control of the arginine regulon in vitro [4].
  • We may conclude that the substitution of 4-fluorotryptophan in arginyl-tRNA synthetase had no substantial effect on the structure and function of the enzyme [5].
 

Other interactions of argS

References

 
WikiGenes - Universities