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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Gene Review: 

FARSB  -  phenylalanyl-tRNA synthetase, beta subunit

Homo sapiens

Synonyms: FARSLB, FRSB, HSPC173, PheHB, PheRS, ...
 
 
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Disease relevance of FARSB

  • The crystal structure of the ternary complex of (alphabeta)(2) heterotetrameric phenylalanyl-tRNA synthetase (PheRS) from Thermus thermophilus with cognate tRNA(Phe) and a nonhydrolyzable phenylalanyl-adenylate analogue (PheOH-AMP) has been determined at 3.1 A resolution [1].
 

High impact information on FARSB

  • First, the mutations of Leu-202, Ser-211, Asp-234, and Thr-236 made the PheRS incorrectly hydrolyze the cognate Phe-tRNA(Phe), indicating that these residues participate in the Tyr hydroxy group recognition and are responsible for discrimination against Phe [2].
  • Our data suggest that the idiosyncratic feature of PheRS, which aminoacylates the 2'-OH group of the terminal ribose, is dictated by the system-specific topology of the CCA end-binding site [1].
  • The functional roles of phenylalanine and ATP in productive binding of the tRNA(Phe) acceptor end have been studied by photoaffinity labeling (cross-linking) of T. thermophilus phenylalanyl-tRNA synthetase (PheRS) with tRNA(Phe) analogs containing the s(4)U residue in different positions of the 3'-terminal single-stranded sequence [3].

References

  1. The crystal structure of the ternary complex of phenylalanyl-tRNA synthetase with tRNAPhe and a phenylalanyl-adenylate analogue reveals a conformational switch of the CCA end. Moor, N., Kotik-Kogan, O., Tworowski, D., Sukhanova, M., Safro, M. Biochemistry (2006) [Pubmed]
  2. Structural and mutational studies of the amino acid-editing domain from archaeal/eukaryal phenylalanyl-tRNA synthetase. Sasaki, H.M., Sekine, S., Sengoku, T., Fukunaga, R., Hattori, M., Utsunomiya, Y., Kuroishi, C., Kuramitsu, S., Shirouzu, M., Yokoyama, S. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  3. Role of low-molecular-weight substrates in functional binding of the tRNAPhe acceptor end by phenylalanyl-tRNA synthetase. Vasil'eva, I.A., Bogachev, V.S., Favre, A., Lavrik, O.I., Moor, N.A. Biochemistry Mosc. (2004) [Pubmed]
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