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Literature summary for 6.1.1.9 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
Search for more literature for 6.1.1.9

Cloned(Commentary)

Cloned (Comment) Organism
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

Protein Variants Comment Organism
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
additional information a knockout mutation causes early larval lethality Caenorhabditis elegans

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Caenorhabditis elegans

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Caenorhabditis elegans Q9U1Q4
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-

Source Tissue

Source Tissue Comment Organism Textmining
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
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Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
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

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

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Caenorhabditis elegans

General Information

General Information Comment Organism
evolution glp-4 VARS-2 is a cytoplasmic class I valyl aminoacyl tRNA synthetase Caenorhabditis elegans
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
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