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Literature summary extracted from

  • Rastogi, S.; Borgo, B.; Pazdernik, N.; Fox, P.; Mardis, E.; Kohara, Y.; Havranek, J.; Schedl, T.
    Caenorhabditis elegans glp-4 encodes a valyl aminoacyl tRNA synthetase (2015), G3 (Bethesda), 5, 2719-2728 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.1.1.9 gene glp-4, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of wild-type and mutant ValRS enzymes in Escherichia coli strain Rosetta (DE3) Caenorhabditis elegans

Protein Variants

EC Number Protein Variants Comment Organism
6.1.1.9 G296D naturally occuring mutation bn2, the mutant glp-4(bn2ts) shows partial loss of function. Aspartate 296 in the editing pocket induces inappropriate deacylation of correctly charged Val-tRNAval. Intragenic suppressor mutations are predicted to displace aspartate 296 so that it is less able to catalyze inappropriate deacylation. Thus glp-4(bn2ts) likely causes reduced protein translation due to decreased levels of Val-tRNAval. glp-4(bn2ts) mutants are widely used to generate germline deficient mutants for organismal studies, under the assumption that the soma is unaffected. As reduced translation has also been demonstrated to alter organismal properties, it is unclear whether changes in aging, stress resistance etc. observed in glp-4(bn2ts) mutants are the result of germline deficiency or reduced translation. The G296D mutation lies just inside a region of the valyl-tRNA synthetase called the CP1 domain Caenorhabditis elegans
6.1.1.9 additional information a knockout mutation causes early larval lethality Caenorhabditis elegans

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.1.1.9 Mg2+ required Caenorhabditis elegans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.1.1.9 ATP + L-valine + tRNAVal Caenorhabditis elegans
-
 AMP + diphosphate + L-valyl-tRNAVal
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.1.1.9 Caenorhabditis elegans Q9U1Q4
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
6.1.1.9 additional information in situ hybridization demonstrates expression of gene glp-4, VARS-2, in the germline and soma, overview. Very strong germline expression is observed in the two U-shaped gonad arms Caenorhabditis elegans
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.1.1.9 ATP + L-valine + tRNAVal
-
 Caenorhabditis elegans AMP + diphosphate + L-valyl-tRNAVal
-
 ?

Subunits

EC Number Subunits Comment Organism
6.1.1.9 More glp-4 VARS-2 has two tRNA recognition domains (1 and 2), a split class 1 Rossmann-fold, which functions in catalyzing the synthesis of aminoacyl-adenylate and aminoacyl-tRNAval, an editing domain, and the connective polypeptide (CP1) domain, which also functions in post-transfer editing. Structural analysis of glp-4 VARS-2, homology modeling, overview Caenorhabditis elegans

Synonyms

EC Number Synonyms Comment Organism
6.1.1.9 glp-4
-
 Caenorhabditis elegans
6.1.1.9 valyl aminoacyl tRNA synthetase
-
 Caenorhabditis elegans
6.1.1.9 VARS-2
-
 Caenorhabditis elegans

Cofactor

EC Number Cofactor Comment Organism Structure
6.1.1.9 ATP
-
 Caenorhabditis elegans

General Information

EC Number General Information Comment Organism
6.1.1.9 evolution glp-4 VARS-2 is a cytoplasmic class I valyl aminoacyl tRNA synthetase Caenorhabditis elegans
6.1.1.9 additional information structure homology modeling using the valine tRNA-synthetase (valRS) from Thermus thermophilius, PDB ID 1IVS, as a template, also with bound valyl-adenylate substrate Caenorhabditis elegans
6.1.1.9 physiological function glp-4 VARS-2 is a cytoplasmic class I valyl aminoacyl tRNA synthetase that catalyzes the transfer of valine to its cognate tRNA for protein synthesis Caenorhabditis elegans