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| Titel: |
Basic Faced α-Helices are Widespread in the Peptide Extensions of the Eukaryotic Aminoacyl-tRNA Synthetases |
| Auteur: |
Massey, Steven E. |
| Verschenen in: |
In silico biology |
| Paginering: | Jaargang 6 (2006) nr. 4 pagina's 259-273 |
| Jaar: |
2006-09-21 |
| Inhoud: |
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. |
| Uitgever: |
IOS Press |
| Bronbestand: |
Elektronische Wetenschappelijke Tijdschriften |
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