{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T15:54:38Z","timestamp":1791129278553,"version":"4.1.0"},"reference-count":46,"publisher":"American Society for Microbiology","issue":"5","license":[{"start":{"date-parts":[[2009,3,1]],"date-time":"2009-03-01T00:00:00Z","timestamp":1235865600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[2009,3]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            The inner membrane BacA protein is essential for the establishment of chronic intracellular infections by\n            <jats:italic>Sinorhizobium meliloti<\/jats:italic>\n            and\n            <jats:italic>Brucella abortus<\/jats:italic>\n            within plant and mammalian hosts, respectively. In their free-living state,\n            <jats:italic>S. meliloti<\/jats:italic>\n            and\n            <jats:italic>B. abortus<\/jats:italic>\n            mutants lacking BacA have reductions in their outer membrane lipid A very-long-chain fatty acid (VLCFA) contents and exhibit low-level resistance to the glycopeptide bleomycin in comparison to their respective parent strains. In this paper we investigate the hypothesis that BacA is involved in peptide uptake in\n            <jats:italic>S. meliloti<\/jats:italic>\n            . We determined that an\n            <jats:italic>S. meliloti<\/jats:italic>\n            \u0394\n            <jats:italic>bacA<\/jats:italic>\n            mutant is completely resistant to a truncated form of the eukaryotic peptide Bac7, Bac7(1-16), and this phenotype appears to be independent of its lipid A alteration. Subsequently, we discovered that BacA and\/or\n            <jats:italic>Escherichia coli<\/jats:italic>\n            SbmA is essential for fluorescently labeled Bac7(1-16) uptake in\n            <jats:italic>S. meliloti<\/jats:italic>\n            . Given that there are hundreds of root nodule-specific peptides within the legume host, our data suggest that BacA-mediated peptide uptake could play a central role in the chronic infection process of\n            <jats:italic>S. meliloti<\/jats:italic>\n            . However, since we determined that two symbiotically defective\n            <jats:italic>S. meliloti bacA<\/jats:italic>\n            site-directed mutants (with the Q193G and R389G mutations, respectively) with known reductions in their lipid A VLCFA contents are still capable of peptide uptake, these findings suggest that BacA-dependent peptide uptake cannot fully account for the essential role of BacA in the legume symbiosis. Further, they provide evidence that the BacA function that leads to the\n            <jats:italic>S. meliloti<\/jats:italic>\n            lipid A VLCFA modification plays a key role in the chronic infection of legumes.\n          <\/jats:p>","DOI":"10.1128\/jb.01661-08","type":"journal-article","created":{"date-parts":[[2008,12,13]],"date-time":"2008-12-13T02:48:38Z","timestamp":1229136518000},"page":"1519-1527","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":84,"title":["Essential Role for the BacA Protein in the Uptake of a Truncated Eukaryotic Peptide in\n            <i>Sinorhizobium meliloti<\/i>"],"prefix":"10.1128","volume":"191","author":[{"given":"Victoria L.","family":"Marlow","sequence":"first","affiliation":[{"name":"School of Medicine &amp; Dentistry, Institute of Medical Sciences, University of Aberdeen, Foresterhill, Aberdeen, AB25 2ZD, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andreas F.","family":"Haag","sequence":"additional","affiliation":[{"name":"School of Medicine &amp; Dentistry, Institute of Medical Sciences, University of Aberdeen, Foresterhill, Aberdeen, AB25 2ZD, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hajime","family":"Kobayashi","sequence":"additional","affiliation":[{"name":"Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vivien","family":"Fletcher","sequence":"additional","affiliation":[{"name":"School of Medicine &amp; Dentistry, Institute of Medical Sciences, University of Aberdeen, Foresterhill, Aberdeen, AB25 2ZD, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marco","family":"Scocchi","sequence":"additional","affiliation":[{"name":"Department of Life Sciences, University of Trieste, Via Giorgieri 1, 34127 Trieste, Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Graham C.","family":"Walker","sequence":"additional","affiliation":[{"name":"Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gail P.","family":"Ferguson","sequence":"additional","affiliation":[{"name":"School of Medicine &amp; Dentistry, Institute of Medical Sciences, University of Aberdeen, Foresterhill, Aberdeen, AB25 2ZD, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"crossref","first-page":"1138","DOI":"10.1094\/MPMI-20-9-1138","volume":"20","year":"2007","unstructured":"Alunni, B., Z. 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