| Autor: |
Gorbalenia AE, Kunin EV, Donchenko AP, Blinov VM |
| Jazyk: |
ruština |
| Zdroj: |
Molekuliarnaia genetika, mikrobiologiia i virusologiia [Mol Gen Mikrobiol Virusol] 1989 Jun (6), pp. 12-6. |
| Abstrakt: |
Analysis of amino acid sequences of barley stripe mosaic virus (BSMV) proteins revealed the pentapeptide GDSGG, the sequence unique for catalytic centers of serine chymotrypsin-like proteases, in protein p14 encoded by open reading frame 4 of RNA beta. Computer-assisted comparisons revealed a statistically significant similarity between amino acid sequences of p14 and chymotrypsin-like proteases. The catalytic His and Asp residues tentatively identified in p14 together with the Ser residue of the GDSGG sequence, presumably, constitute the "catalytic triad" characteristic of chymotrypsin-like proteases. Based on these observations and on the presence of a potential N-proximal transmembrane domain in p14, this protein may be suggested to be a serine protease involved in processing of the replicase precursor within a membrane-bound replication complex of BSMV. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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