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Synthases called penicillin\u2010binding proteins (\n                    <jats:styled-content style=\"fixed-case\">PBPs<\/jats:styled-content>\n                    ), the targets of penicillin and related antibiotics, polymerize the glycan strands of\n                    <jats:styled-content style=\"fixed-case\">PG<\/jats:styled-content>\n                    and crosslink them into the cell wall meshwork via attached peptides. The average length of glycan chains inserted into the matrix by the\n                    <jats:styled-content style=\"fixed-case\">PBPs<\/jats:styled-content>\n                    is thought to play an important role in bacterial morphogenesis, but polymerization termination factors controlling this process have yet to be discovered. Here, we report the identification of\n                    <jats:styled-content style=\"fixed-case\">\n                      <jats:italic>E<\/jats:italic>\n                    <\/jats:styled-content>\n                    <jats:italic>scherichia coli<\/jats:italic>\n                    \u2005\n                    <jats:styled-content style=\"fixed-case\">MltG<\/jats:styled-content>\n                    (\n                    <jats:styled-content style=\"fixed-case\">YceG<\/jats:styled-content>\n                    ) as a potential terminase for glycan polymerization that is broadly conserved in bacteria. A clone containing\n                    <jats:italic>mltG<\/jats:italic>\n                    was initially isolated in a screen for multicopy plasmids generating a lethal phenotype in cells defective for the\n                    <jats:styled-content style=\"fixed-case\">PG<\/jats:styled-content>\n                    synthase\n                    <jats:styled-content style=\"fixed-case\">PBP1b<\/jats:styled-content>\n                    . Biochemical studies revealed that\n                    <jats:styled-content style=\"fixed-case\">MltG<\/jats:styled-content>\n                    is an inner membrane enzyme with endolytic transglycosylase activity capable of cleaving at internal positions within a glycan polymer. Radiolabeling experiments further demonstrated\n                    <jats:styled-content style=\"fixed-case\">MltG<\/jats:styled-content>\n                    \u2010dependent nascent\n                    <jats:styled-content style=\"fixed-case\">PG<\/jats:styled-content>\n                    processing\n                    <jats:italic>in vivo<\/jats:italic>\n                    , and bacterial two\u2010hybrid analysis identified an\n                    <jats:styled-content style=\"fixed-case\">MltG<\/jats:styled-content>\n                    \u2010PBP1b interaction. Mutants lacking\n                    <jats:styled-content style=\"fixed-case\">MltG<\/jats:styled-content>\n                    were also shown to have longer glycans in their\n                    <jats:styled-content style=\"fixed-case\">PG<\/jats:styled-content>\n                    relative to wild\u2010type cells. Our combined results are thus consistent with a model in which\n                    <jats:styled-content style=\"fixed-case\">MltG<\/jats:styled-content>\n                    associates with\n                    <jats:styled-content style=\"fixed-case\">PG<\/jats:styled-content>\n                    synthetic complexes to cleave nascent polymers and terminate their elongation.\n                  <\/jats:p>","DOI":"10.1111\/mmi.13258","type":"journal-article","created":{"date-parts":[[2015,10,28]],"date-time":"2015-10-28T02:36:04Z","timestamp":1445999764000},"page":"700-718","source":"Crossref","is-referenced-by-count":139,"title":["Identification of MltG as a potential terminase for peptidoglycan polymerization in bacteria"],"prefix":"10.1111","volume":"99","author":[{"given":"Rachel","family":"Yunck","sequence":"first","affiliation":[{"name":"Department of Microbiology and Immunobiology Harvard Medical School  Boston MA 02115 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