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« Previous AbstractTarget identification of volatile metabolites to allow the differentiation of lactic acid bacteria by gas chromatography-ion mobility spectrometry    Next AbstractTranscriptional control of sex-pheromone-inducible genes on plasmid pAD1 of Enterococcus faecalis and sequence analysis of a third structural gene for (pPD1-encoded) aggregation substance »

Mol Microbiol


Title:Sequence analysis of Enterococcus faecalis aggregation substance encoded by the sex pheromone plasmid pAD1
Author(s):Galli D; Lottspeich F; Wirth R;
Address:"Lehrstuhl fur Mikrobiologie der Universitat Munchen, FRG"
Journal Title:Mol Microbiol
Year:1990
Volume:4
Issue:6
Page Number:895 - 904
DOI: 10.1111/j.1365-2958.1990.tb00662.x
ISSN/ISBN:0950-382X (Print) 0950-382X (Linking)
Abstract:"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 (named asa1) was found to code for a protein of 1296 amino acids (Mr 142,248). 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"
Keywords:"Amino Acid Sequence Bacterial Adhesion Bacterial Proteins/biosynthesis/*genetics Base Sequence DNA, Bacterial/analysis Enterococcus faecalis/*genetics Molecular Sequence Data Plasmids/*genetics Sequence Homology, Nucleic Acid Sex Attractants/biosynthesis/;"
Notes:"MedlineGalli, D Lottspeich, F Wirth, R eng Research Support, Non-U.S. Gov't England 1990/06/01 Mol Microbiol. 1990 Jun; 4(6):895-904. doi: 10.1111/j.1365-2958.1990.tb00662.x"

 
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