SEQUENCE-ANALYSIS OF ENTEROCOCCUS-FAECALIS AGGREGATION SUBSTANCE ENCODED BY THE SEX-PHEROMONE PLASMID PAD1
SEQUENCE-ANALYSIS OF ENTEROCOCCUS-FAECALIS AGGREGATION SUBSTANCE ENCODED BY THE SEX-PHEROMONE PLASMID PAD1
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DOI:
10.1111/j.1365-2958.1990.tb00662.x
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发表时间:
1990-06-01
影响因子:
3.6
通讯作者:
WIRTH, R
中科院分区:
文献类型:
--
作者:
GALLI, D;LOTTSPEICH, F;WIRTH, R
The location of the structural gene for aggregation substance on the sex pheromone plasmid pAD1 of Enterococcus faecalis was determined using an oligonucleotide deduced from the N-terminal amino acid sequence of the purified protein. The nucleotide sequence was determined for the corresponding region and two open reading frames (ORFs) could be identified. ORF1 codes for a small (Mr 13 160) acidic protein of unknown function. The gene for aggregation substance (names asa1) was found to code for a protein of 1296 amino acids (Mr 142248). The protein has a signal peptide of 43 amino acids (the resulting Mr for mature aggregation substance is 137 429) and contains in its C-terminal region a proline-rich sequence, previously characterized as being involved in cell wall association, which is followed by a membrane anchor. The membrane anchor showed significant similarity to that of other Gram-positive organisms, but no other similarities to surface proteins from Gram-positive bacteria were found. In particular, no repeats on the DNA or protein level could be detected for pAD1-specific aggregation substance. The protein contains the amino acid motifs Arg-Gly-Asp-Ser and Arg-Gly-Asp-Val (once each), which, it is proposed, play a crucial role in adherence to eukaryotic cells.