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- Title
Basic Faced α-Helices are Widespread in the Peptide Extensions of the Eukaryotic Aminoacyl-tRNA Synthetases.
- Authors
Massey, Steven E.
- Abstract
Three aminoacyl-tRNA synthetases from yeast, one from plants and one from mammals possess unusual structures at their N termini, namely α helices with basic residues distributed asymmetrically, on a single face of the helix. It is unknown if these 'basic faced' α helices (BFAHs) are unique to the aminoacyl-tRNA synthetases. Analysis of the amino acid sequences of these five aminoacyl-tRNA synthetases using the hydrophobic moment algorithm failed to accurately identify the BFAHs. A new algorithm was therefore developed, called the 'basic moment'. This is a Fourier analysis procedure that predicts the distribution of basic residues within protein secondary structure. The basic moment identifies with a high degree of accuracy the five known BFAHs and also identifies further potential BFAHs at evolutionarily conserved positions in the peptide extensions of aspartyl-, lysyl- and valyl- tRNA synthetases from a range of eukaryotic species. In addition, the algorithm identifies the two-helix pair tRNA binding domain of alanyl-tRNA synthetase, implying that the domain includes a BFAH. The functional and evolutionary aspects of these structural features are discussed.
- Subjects
PEPTIDES; TRANSFER RNA; YEAST; AMINO acid sequence; MOLECULAR structure
- Publication
In Silico Biology, 2006, Vol 6, Issue 4, p259
- ISSN
1386-6338
- Publication type
Article