Difference between revisions of "PMID:8631687"
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| + | {| id="D5055086a98e69" class=" tableEdit PMID_info_table" | ||
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| + | !align=left |Citation | ||
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| + | '''Kawagishi, I , Homma, M , Williams, AW and Macnab, RM ''' (1996) Characterization of the flagellar hook length control protein fliK of Salmonella typhimurium and Escherichia coli. ''J. Bacteriol.'' '''178''':2954-9 | ||
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| + | !align=left |Abstract | ||
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| + | During flagellar morphogenesis in Salmonella typhimurium and Escherichia coli, the fliK gene product is responsible for hook length control. A previous study (M. Homma, T. Iino, and R. M. Macnab, J. Bacteriol. 170:2221-2228, 1988) had suggested that the fliK gene may generate two products; we have confirmed that both proteins are products of the fliK gene and have eliminated several possible explanations for the two forms. We have determined the DNA sequence of the fliK gene in both bacterial species. The deduced amino acid sequences of the wild-type FliK proteins of S. typhimurium and E. coli correspond to molecular masses of 41,748 and 39,246 Da, respectively, and are fairly hydrophilic. Alignment of the sequences gives an identity level of 50%, which is low for homologous flagellar proteins from S. typhimurium and E. coli; the C-terminal sequence is the most highly conserved part (71% identity in the last 154 amino acids). The central and C-terminal regions are rich in proline and glutamine residues, respectively. Linker insertion mutagenesis of the conserved C-terminal region completely abolished motility, whereas disruption of the less conserved N-terminal and central regions had little or no effect. We suggest that the N-terminal (or N-terminal and central) and C-terminal regions may constitute domains. For several reasons, we consider it unlikely that FliK is functioning as a molecular ruler for determining hook length and conclude that it is probably employing a novel mechanism. | ||
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| + | !align=left |Links | ||
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| + | [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8631687 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC178034 PMC178034] | ||
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| + | !align=left |Keywords | ||
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| + | Amino Acid Sequence; Bacterial Proteins/genetics; Base Sequence; Escherichia coli/cytology; Escherichia coli/genetics; Escherichia coli Proteins; Flagella/genetics; Genes, Bacterial; Molecular Sequence Data; Morphogenesis; Mutagenesis, Insertional; Polymorphism, Genetic; Salmonella typhimurium/cytology; Salmonella typhimurium/genetics; Sequence Analysis, DNA; Species Specificity | ||
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| + | <!--box uid=d41d8cd98f00b204e9800998ecf8427e.3372.D5055086a98e69--> | ||
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| + | ==Main Points of the Paper == | ||
| + | {{LitSignificance}} | ||
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| + | == Materials and Methods Used == | ||
| + | {{LitMaterials}} | ||
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| + | ==Phenotype Annotations== | ||
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| + | {| id="K5055086aa4d04" class=" tableEdit Phenotype_Table_2" | ||
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| + | !|Phenotype of!!Taxon Information!!Genotype Information (if known)!!Condition Information!!OMP ID!!OMP Term Name!!ECO ID!!ECO Term Name!!Notes!!Status | ||
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| + | <!--box uid=d41d8cd98f00b204e9800998ecf8427e.3372.K5055086aa4d04--></protect> | ||
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| + | ==Notes== | ||
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| + | ==References== | ||
| + | {{RefHelp}} | ||
| + | <references/> | ||
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| + | [[Category:Publication]] | ||
Latest revision as of 17:59, 15 September 2012
| Citation |
Kawagishi, I , Homma, M , Williams, AW and Macnab, RM (1996) Characterization of the flagellar hook length control protein fliK of Salmonella typhimurium and Escherichia coli. J. Bacteriol. 178:2954-9 |
|---|---|
| Abstract |
During flagellar morphogenesis in Salmonella typhimurium and Escherichia coli, the fliK gene product is responsible for hook length control. A previous study (M. Homma, T. Iino, and R. M. Macnab, J. Bacteriol. 170:2221-2228, 1988) had suggested that the fliK gene may generate two products; we have confirmed that both proteins are products of the fliK gene and have eliminated several possible explanations for the two forms. We have determined the DNA sequence of the fliK gene in both bacterial species. The deduced amino acid sequences of the wild-type FliK proteins of S. typhimurium and E. coli correspond to molecular masses of 41,748 and 39,246 Da, respectively, and are fairly hydrophilic. Alignment of the sequences gives an identity level of 50%, which is low for homologous flagellar proteins from S. typhimurium and E. coli; the C-terminal sequence is the most highly conserved part (71% identity in the last 154 amino acids). The central and C-terminal regions are rich in proline and glutamine residues, respectively. Linker insertion mutagenesis of the conserved C-terminal region completely abolished motility, whereas disruption of the less conserved N-terminal and central regions had little or no effect. We suggest that the N-terminal (or N-terminal and central) and C-terminal regions may constitute domains. For several reasons, we consider it unlikely that FliK is functioning as a molecular ruler for determining hook length and conclude that it is probably employing a novel mechanism. |
| Links | |
| Keywords |
Amino Acid Sequence; Bacterial Proteins/genetics; Base Sequence; Escherichia coli/cytology; Escherichia coli/genetics; Escherichia coli Proteins; Flagella/genetics; Genes, Bacterial; Molecular Sequence Data; Morphogenesis; Mutagenesis, Insertional; Polymorphism, Genetic; Salmonella typhimurium/cytology; Salmonella typhimurium/genetics; Sequence Analysis, DNA; Species Specificity |
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Main Points of the Paper
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Materials and Methods Used
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<protect>
| Phenotype of | Taxon Information | Genotype Information (if known) | Condition Information | OMP ID | OMP Term Name | ECO ID | ECO Term Name | Notes | Status |
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</protect>
Notes
References
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