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| Content Provider | PubMed Central |
|---|---|
| Author | Mora, Javier De La Ballado, Teresa Bertha, González-pedrajo Camarena, Laura Dreyfus, Georges |
| Abstract | We have characterized open reading frame RSP0072, which is located within the flgG operon in Rhodobacter sphaeroides. The amino acid sequence analysis of this gene product showed the presence of a soluble lytic transglycosylase domain. The deletion of the N-terminal region (90 amino acids) of the product of RSP0072 yields a leaky nonmotile phenotype, as determined by swarm assays in soft agar. Electron micrographs revealed the lack of flagella in mutant cells. The purified wild-type protein showed lytic activity on extracts of Micrococcus luteus. In contrast, no lytic activity was observed when the residues E57 or E83 were replaced by alanine. Affinity blotting suggests that the protein encoded by RSP0072 interacts with the flagellar rod-scaffolding protein FlgJ, which lacks the muramidase domain present in FlgJ of many bacteria. We propose that the product of RSP0072 is a flagellar muramidase that is exported to the periplasm via the Sec pathway, where it interacts with FlgJ to open a gap in the peptidoglycan layer for the subsequent penetration of the nascent flagellar structure. |
| Related Links | http://dx.doi.org/10.1128/jb.01073-07 |
| Ending Page | 8004 |
| Page Count | 7 |
| Starting Page | 7998 |
| File Format | |
| ISSN | 00219193 |
| e-ISSN | 10985530 |
| Journal | Journal of Bacteriology |
| Issue Number | 22 |
| Volume Number | 189 |
| Language | English |
| Publisher | American Society for Microbiology (ASM) |
| Publisher Date | 2007-11-15 |
| Access Restriction | Open |
| Rights Holder | American Society for Microbiology (ASM) |
| Subject Keyword | Molecular Biology Microbiology Research in Higher Education |
| Content Type | Text |
| Resource Type | Article |
| Subject | Molecular Biology Microbiology |
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