| pubmed-article:7635816 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7635816 | lifeskim:mentions | umls-concept:C0315286 | lld:lifeskim |
| pubmed-article:7635816 | lifeskim:mentions | umls-concept:C0030958 | lld:lifeskim |
| pubmed-article:7635816 | lifeskim:mentions | umls-concept:C0001038 | lld:lifeskim |
| pubmed-article:7635816 | lifeskim:mentions | umls-concept:C0288397 | lld:lifeskim |
| pubmed-article:7635816 | lifeskim:mentions | umls-concept:C1880177 | lld:lifeskim |
| pubmed-article:7635816 | pubmed:issue | 15 | lld:pubmed |
| pubmed-article:7635816 | pubmed:dateCreated | 1995-9-13 | lld:pubmed |
| pubmed-article:7635816 | pubmed:abstractText | A collection of Providencia stuartii mutants which either underexpress or overexpress aac(2')-Ia, the chromosomal gene coding for gentamicin 2'-N-acetyltransferase (EC 2.3.1.59), have been characterized phenotypically as possessing either lower or higher levels of peptidoglycan O acetylation, respectively, than the wild type. These mutants were subjected to both negative-staining and thin-section electron microscopy. P. stuartii PR100, with 42% O acetylation of peptidoglycan compared with 52% O acetylation in the wild type, appeared as irregular rods. In direct contrast, P. stuartii strains PR50.LM3 and PR51, with increased levels of peptidoglycan O acetylation (65 and 63%, respectively), appeared as coccobacilli and chain formers, respectively. Membrane blebbing was also observed with the chain-forming strain PR51. Thin sectioning of this mutant indicated that it was capable of proper constriction and separation. P. stuartii PM1, when grown to mid-exponential phase, did not have altered peptidoglycan O-acetylation levels, and cellular morphology remained similar to that of wild-type strains. However, continued growth into stationary phase resulted in a 15% increase in peptidoglycan O acetylation concomitant with a change of some cells from a rod-shaped to a coccobacillus-shaped morphology. The fact that these apparent morphological changes were directly related to levels of O acetylation support the view that this modification plays a role in the maintenance of peptidoglycan structure, presumably through the control of autolytic activity. | lld:pubmed |
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| pubmed-article:7635816 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7635816 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7635816 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7635816 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7635816 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:7635816 | pubmed:issn | 0021-9193 | lld:pubmed |
| pubmed-article:7635816 | pubmed:author | pubmed-author:ClarkeA JAJ | lld:pubmed |
| pubmed-article:7635816 | pubmed:author | pubmed-author:RatherP NPN | lld:pubmed |
| pubmed-article:7635816 | pubmed:author | pubmed-author:PayieK GKG | lld:pubmed |
| pubmed-article:7635816 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7635816 | pubmed:volume | 177 | lld:pubmed |
| pubmed-article:7635816 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7635816 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7635816 | pubmed:pagination | 4303-10 | lld:pubmed |
| pubmed-article:7635816 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:7635816 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7635816 | pubmed:articleTitle | Contribution of gentamicin 2'-N-acetyltransferase to the O acetylation of peptidoglycan in Providencia stuartii. | lld:pubmed |
| pubmed-article:7635816 | pubmed:affiliation | Department of Microbiology, University of Guelph, Ontario, Canada. | lld:pubmed |
| pubmed-article:7635816 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7635816 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:7635816 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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