| the n-terminal region of the oenococcus oeni bacteriophage fog44 lysin behaves as a bona fide signal peptide in escherichia coli and as a cis-inhibitory element, preventing lytic activity on oenococcal cells. | the function of the n-terminal region of the oenococcus oeni phage fog44 lysin (lys44) as an export signal was investigated. we observed that when induced in escherichia coli, lys44 was cleaved between residues 27 and 28 in a seca-dependent manner. lys44 processing could be blocked by a specific signal peptidase inhibitor and was severely reduced by modification of the cleavage site. the lethal effect of lys44 expression observed in e. coli was ascribed to the presence of its n-terminal 27-resid ... | 2000 | 11004183 |
| gene organization in a central dna fragment of oenococcus oeni bacteriophage fog44 encoding lytic, integrative and non-essential functions. | the nucleotide sequence of a dna fragment previously shown to contain the attachment site (attp) of oenococcus oeni phage fog44 (. arch. virol. 143, 523-536) has been determined. sequence analysis indicated that this 6226bp ecori fragment harbours an integrase gene, in the vicinity of a direct repeat rich region defining attp, as well as genes encoding a muramidase-related lysin (lys) and a holin polypeptide (hol). transcriptional studies suggested that lys and hol are mainly co-expressed, late ... | 1999 | 9889328 |