Identification and Characterization of a New Lipoprotein, NlpI, in Escherichia coli K-12
| Autor: | Paul D. Rick, Krishnan Sankaran, Masaru Ohara, Henry C. Wu |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
DNA
Bacterial Cell division Lipoproteins Molecular Sequence Data Mutant Cell Surfaces Biology medicine.disease_cause Microbiology Escherichia coli medicine Amino Acid Sequence Polynucleotide phosphorylase Cloning Molecular Molecular Biology Gene Mutation Escherichia coli Proteins Structural gene Sequence Analysis DNA RNA Helicase A Molecular biology Phenotype Genes Bacterial |
| Zdroj: | Journal of Bacteriology. 181:4318-4325 |
| ISSN: | 1098-5530 0021-9193 |
| DOI: | 10.1128/jb.181.14.4318-4325.1999 |
| Popis: | We report here the identification of a new lipoprotein, NlpI, in Escherichia coli K-12. The NlpI structural gene ( nlpI ) is located between the genes pnp (polynucleotide phosphorylase) and deaD (RNA helicase) at 71 min on the E. coli chromosome. The nlpI gene encodes a putative polypeptide of approximately 34 kDa, and multiple lines of evidence clearly demonstrate that NlpI is indeed a lipoprotein. An nlpI :: cm mutation rendered growth of the cells osmotically sensitive, and incubation of the insertion mutant at an elevated temperature resulted in the formation of filaments. The altered phenotype of the mutant was a direct consequence of the mutation in nlpI , since it was complemented by the wild-type nlpI gene alone. Overexpression of the unaltered nlpI gene in wild-type cells resulted in the loss of the rod morphology and the formation of single prolate ellipsoids and pairs of prolate ellipsoids joined by partial constrictions. NlpI may be important for an as-yet-undefined step in the overall process of cell division. |
| Databáze: | OpenAIRE |
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