Transmembrane Topology of AgrB, the Protein Involved in the Post-translational Modification of AgrD in Staphylococcus aureus *
Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 277, Issue: 38, Page: 34736-34742
2002
- 103Citations
- 100Captures
- 1Mentions
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations103
- Citation Indexes103
- CrossRef103
- 101
- Captures100
- Readers100
- 100
- Mentions1
- News Mentions1
- News1
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Article Description
The accessory gene regulator ( agr ) of Staphylococcus aureus is the central regulatory system that controls the gene expression for a large set of virulence factors. This global regulatory locus consists of two transcripts: RNAII and RNAIII. RNAII encodes four genes ( agrA, B, C, and D ) whose gene products assemble a quorum sensing system. RNAIII is the effector of the Agr response. Both the agrB and agrD genes are essential for the production of the autoinducing peptide, which functions as a signal for the quorum sensing system. In this study, we demonstrated the transmembrane nature of AgrB protein in S. aureus. A transmembrane topology model of AgrB was proposed based on AgrB-PhoA fusion analyses in Escherichia coli. Two hydrophilic regions with several highly conserved positively charged amino acid residues among various AgrBs were found to be located in the cytoplasmic membrane as suggested by PhoA-AgrB fusion studies. However, this finding is inconsistent with the putative transmembrane profile of AgrB by computer analysis. Furthermore, we detected an intermediate peptide of processed AgrD from S. aureus cells expressing AgrB and a 6 histidine-tagged AgrD. These results provide direct evidence that AgrB is involved in the proteolytic processing of AgrD. We speculate that AgrB is a novel protein with proteolytic enzyme activity and a transporter facilitating the export of the processed AgrD peptide.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0021925818366936; http://dx.doi.org/10.1074/jbc.m205367200; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0037144484&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/12122003; http://www.jbc.org/lookup/doi/10.1074/jbc.M205367200; https://syndication.highwire.org/content/doi/10.1074/jbc.M205367200; https://linkinghub.elsevier.com/retrieve/pii/S0021925818366936; https://dx.doi.org/10.1074/jbc.m205367200
American Society for Biochemistry & Molecular Biology (ASBMB)
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