Difference between revisions of "PMID:12787347"
(New PMID: Page!) |
(Fill PMID: Page!) |
||
| Line 1: | Line 1: | ||
| − | + | {{RightTOC}} | |
| + | |||
| + | <!--box uid=d41d8cd98f00b204e9800998ecf8427e.14842.Z598b49ab22c37--> | ||
| + | <!-- | ||
| + | ****************************************************************************************** | ||
| + | * | ||
| + | * ** PLEASE DON'T EDIT THIS TABLE DIRECTLY. Use the edit table link under the table. ** | ||
| + | * | ||
| + | ****************************************************************************************** --> | ||
| + | {| id="Z598b49ab22c37" class=" tableEdit PMID_info_table" | ||
| + | |||
| + | |- | ||
| + | !align=left align='left' bgcolor='#CCCCFF' |Citation | ||
| + | || | ||
| + | '''Bernhardt, TG and de Boer, PA''' (2003) The Escherichia coli amidase AmiC is a periplasmic septal ring component exported via the twin-arginine transport pathway. ''Mol. Microbiol.'' '''48''':1171-82 | ||
| + | |- | ||
| + | !align=left align='left' bgcolor='#CCCCFF' |Abstract | ||
| + | || | ||
| + | The N-acetylmuramoyl-l-alanine amidases of Escherichia coli (AmiA, B and C) are periplasmic enzymes that remove murein cross-links by cleaving the peptide moiety from N-acetylmuramic acid. Ami- cells form chains, indicating that the amidases help to split the septal murein. Interestingly, cells defective in the twin-arginine protein transport (Tat) pathway show a similar division defect. We find that both AmiA and AmiC are routed to the periplasm via Tat, providing an explanation for the Tat- division phenotype. Taking advantage of the ability of Tat to export prefolded (fluorescent) green fluorescent protein (GFP) to the periplasm, we sublocalized AmiA and AmiC in live cells using functional fusions to GFP. Interestingly, the periplasmic localization of the fusions differed markedly. AmiA-GFP appeared to be dispersed throughout the periplasm in all cells. AmiC-GFP similarly appeared throughout the periplasm in small cells, but was concentrated almost exclusively at the septal ring in constricting cells. Recruitment of AmiC to the ring was mediated by an N-terminal non-amidase targeting domain and required the septal ring component FtsN. AmiC therefore replaces FtsN as the latest known recruit to the septal ring and is the first entirely periplasmic component to be localized. | ||
| + | |- | ||
| + | !align=left align='left' bgcolor='#CCCCFF' |Links | ||
| + | || | ||
| + | [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=12787347 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4428285 PMC4428285] | ||
| + | |||
| + | |- | ||
| + | !align=left align='left' bgcolor='#CCCCFF' |Keywords | ||
| + | || | ||
| + | Amino Acid Sequence; Cell Division; Escherichia coli/enzymology; Escherichia coli/physiology; Escherichia coli Proteins/metabolism; Green Fluorescent Proteins; Luminescent Proteins/genetics; Luminescent Proteins/metabolism; Membrane Proteins; Membrane Transport Proteins/metabolism; Molecular Sequence Data; N-Acetylmuramoyl-L-alanine Amidase/chemistry; N-Acetylmuramoyl-L-alanine Amidase/genetics; N-Acetylmuramoyl-L-alanine Amidase/metabolism; Periplasm/enzymology; Protein Transport; Recombinant Fusion Proteins/metabolism | ||
| + | |||
| + | |- class="tableEdit_footer" | ||
| + | |<div class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.14842.Z598b49ab22c37&page=14842&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table]</div> || | ||
| + | |} | ||
| + | <!--box uid=d41d8cd98f00b204e9800998ecf8427e.14842.Z598b49ab22c37--> | ||
| + | |||
| + | ==Main Points of the Paper == | ||
| + | {{LitSignificance}} | ||
| + | |||
| + | == Materials and Methods Used == | ||
| + | {{LitMaterials}} | ||
| + | |||
| + | ==Phenotype Annotations== | ||
| + | {{AnnotationTableHelp}} | ||
| + | <protect><!--box uid=d41d8cd98f00b204e9800998ecf8427e.14842.D598b49ab34695--> | ||
| + | <!-- | ||
| + | ****************************************************************************************** | ||
| + | * | ||
| + | * ** PLEASE DON'T EDIT THIS TABLE DIRECTLY. Use the edit table link under the table. ** | ||
| + | * | ||
| + | ****************************************************************************************** --> | ||
| + | {| border="2" cellpadding="4" cellspacing="0" style="margin: 1em 1em 1em 0; border: 1px #aaa solid; border-collapse: collapse;" id="D598b49ab34695" class=" tableEdit Phenotype_Table_2" | ||
| + | |- align='left' bgcolor='#CCCCFF' | ||
| + | !|Phenotype of!!Taxon Information!!Genotype Information (if known)!!Condition Information!!OMP ID!!OMP Term Name!!ECO ID!!ECO Term Name!!Notes!!Status | ||
| + | |||
| + | |- class="tableEdit_footer" | ||
| + | |<div class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.14842.D598b49ab34695&page=14842&pagename={{FULLPAGENAMEE}}&type=0&template=Phenotype_Table_2 edit table]</div> || || || || || || || || || | ||
| + | |} | ||
| + | <!--box uid=d41d8cd98f00b204e9800998ecf8427e.14842.D598b49ab34695--></protect> | ||
| + | |||
| + | ==Notes== | ||
| + | |||
| + | ==References== | ||
| + | {{RefHelp}} | ||
| + | <references/> | ||
| + | |||
| + | |||
| + | [[Category:Publication]] | ||
Latest revision as of 12:43, 9 August 2017
| Citation |
Bernhardt, TG and de Boer, PA (2003) The Escherichia coli amidase AmiC is a periplasmic septal ring component exported via the twin-arginine transport pathway. Mol. Microbiol. 48:1171-82 |
|---|---|
| Abstract |
The N-acetylmuramoyl-l-alanine amidases of Escherichia coli (AmiA, B and C) are periplasmic enzymes that remove murein cross-links by cleaving the peptide moiety from N-acetylmuramic acid. Ami- cells form chains, indicating that the amidases help to split the septal murein. Interestingly, cells defective in the twin-arginine protein transport (Tat) pathway show a similar division defect. We find that both AmiA and AmiC are routed to the periplasm via Tat, providing an explanation for the Tat- division phenotype. Taking advantage of the ability of Tat to export prefolded (fluorescent) green fluorescent protein (GFP) to the periplasm, we sublocalized AmiA and AmiC in live cells using functional fusions to GFP. Interestingly, the periplasmic localization of the fusions differed markedly. AmiA-GFP appeared to be dispersed throughout the periplasm in all cells. AmiC-GFP similarly appeared throughout the periplasm in small cells, but was concentrated almost exclusively at the septal ring in constricting cells. Recruitment of AmiC to the ring was mediated by an N-terminal non-amidase targeting domain and required the septal ring component FtsN. AmiC therefore replaces FtsN as the latest known recruit to the septal ring and is the first entirely periplasmic component to be localized. |
| Links | |
| Keywords |
Amino Acid Sequence; Cell Division; Escherichia coli/enzymology; Escherichia coli/physiology; Escherichia coli Proteins/metabolism; Green Fluorescent Proteins; Luminescent Proteins/genetics; Luminescent Proteins/metabolism; Membrane Proteins; Membrane Transport Proteins/metabolism; Molecular Sequence Data; N-Acetylmuramoyl-L-alanine Amidase/chemistry; N-Acetylmuramoyl-L-alanine Amidase/genetics; N-Acetylmuramoyl-L-alanine Amidase/metabolism; Periplasm/enzymology; Protein Transport; Recombinant Fusion Proteins/metabolism |
Main Points of the Paper
Please summarize the main points of the paper.
Materials and Methods Used
Please list the materials and methods used in this paper (strains, plasmids, antibodies, etc).
Phenotype Annotations
See Help:AnnotationTable for details on how to edit this table.
<protect>
| Phenotype of | Taxon Information | Genotype Information (if known) | Condition Information | OMP ID | OMP Term Name | ECO ID | ECO Term Name | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|
</protect>
Notes
References
See Help:References for how to manage references in omp dev.
