| pubmed-article:8631709 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8631709 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:8631709 | lifeskim:mentions | umls-concept:C0007590 | lld:lifeskim |
| pubmed-article:8631709 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:8631709 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:8631709 | lifeskim:mentions | umls-concept:C0205224 | lld:lifeskim |
| pubmed-article:8631709 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:8631709 | pubmed:dateCreated | 1996-7-3 | lld:pubmed |
| pubmed-article:8631709 | pubmed:abstractText | Genetic and biochemical approaches were used to analyze a topological model for FtsN, a 36-kDa protein with a putative transmembrane segment near the N terminus, and to ascertain the requirements of the putative cytoplasmic and membrane-spanning domains for the function of this protein. Analysis of FtsN-PhoA fusions revealed that the putative transmembrane segment of FtsN could act as a translocation signal. Protease accessibility studies of FtsN in spheroblasts and inverted membrane vesicles confirmed that FtsN had a simple bitopic topology with a short cytoplasmic amino terminus, a single membrane-spanning domain, and a large periplasmic carboxy terminus. To ascertain the functional requirements of the N-terminal segments of FtsN, various constructs were made. Deletion of the N-terminal cytoplasmic and membrane-spanning domains led to intracellular localization of the carboxy domain, instability,and loss of function. Replacement of the N-terminal cytoplasmic and membrane-spanning domains with a membrane-spanning domain from MalG restored subcellular localization and function. These N-terminal domains of FtsN could also be replaced by the cleavable MalE signal sequence with restoration of subcellular localization and function. It is concluded that the N-terminal, cytoplasmic, and transmembrane domains of FtsN are not required for function of the carboxy domain other than to transport it to the periplasm. FtsQ and FtsI were also analyzed. | lld:pubmed |
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| pubmed-article:8631709 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:8631709 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8631709 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8631709 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:8631709 | pubmed:issn | 0021-9193 | lld:pubmed |
| pubmed-article:8631709 | pubmed:author | pubmed-author:DamWW | lld:pubmed |
| pubmed-article:8631709 | pubmed:author | pubmed-author:XuYY | lld:pubmed |
| pubmed-article:8631709 | pubmed:author | pubmed-author:LutkenhausJJ | lld:pubmed |
| pubmed-article:8631709 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8631709 | pubmed:volume | 178 | lld:pubmed |
| pubmed-article:8631709 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8631709 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8631709 | pubmed:pagination | 1328-34 | lld:pubmed |
| pubmed-article:8631709 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:8631709 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8631709 | pubmed:articleTitle | Topological characterization of the essential Escherichia coli cell division protein FtsN. | lld:pubmed |
| pubmed-article:8631709 | pubmed:affiliation | Department of Microbiology, Molecular Genetics, and Immunology, University of Kansas Medical Center, Kansas City 66160, USA. | lld:pubmed |
| pubmed-article:8631709 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8631709 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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