Difference between revisions of "PMID:15063851"
(New PMID: Page!) |
(Fill PMID: Page!) |
||
Line 1: | Line 1: | ||
+ | {{RightTOC}} | ||
+ | <!--box uid=d41d8cd98f00b204e9800998ecf8427e.4170.F5230d73fef6b8--> | ||
+ | <!-- | ||
+ | ****************************************************************************************** | ||
+ | * | ||
+ | * ** PLEASE DON'T EDIT THIS TABLE DIRECTLY. Use the edit table link under the table. ** | ||
+ | * | ||
+ | ****************************************************************************************** --> | ||
+ | {| id="F5230d73fef6b8" class=" tableEdit PMID_info_table" | ||
+ | |||
+ | |- | ||
+ | !align=left align='left' bgcolor='#CCCCFF' |Citation | ||
+ | || | ||
+ | '''No author listed''' (2004) Control of SecA and SecM translation by protein secretion. ''Curr. Opin. Microbiol.'' '''7''':145-50 | ||
+ | |- | ||
+ | !align=left align='left' bgcolor='#CCCCFF' |Abstract | ||
+ | || | ||
+ | SecA, the protein translocation ATPase of E. coli is subject to secretion-defect-response control. SecM (secretion monitor) encoded by the 5' region of the secM-secA mRNA is involved in this regulation. SecM translation is subject to transient elongation arrest at Pro166, which is prolonged when export of the nascent SecM is blocked. An "arrest sequence", FXXXXWIXXXXGIRAGP, was identified at a carboxy-terminal region of SecM that interacts with the ribosomal exit tunnel. Presumably, the stalled ribosome disrupts the secondary structure of the secM-secA mRNA such that the Shine-Dalgarno sequence for translation of secA is exposed. Mutation studies established that the SecM elongation arrest is required for the viability of E. coli as well as for constitutive (in secretion-proficient cells) and upregulated (in secretion compromised cells) expression of SecA. Furthermore, evidence suggests that elongation-arresting SecM has a role of upregulating the functionality of newly synthesized SecA molecules, presumably by bringing the mRNA to the vicinity of the membrane/Sec translocation apparatus. These results are discussed in relation to the versatile nature of SecA in its localization and structure. | ||
+ | |- | ||
+ | !align=left align='left' bgcolor='#CCCCFF' |Links | ||
+ | || | ||
+ | [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=15063851 PubMed] | ||
+ | Online version:[http://dx.doi.org/10.1016/j.mib.2004.01.001 10.1016/j.mib.2004.01.001] | ||
+ | |- | ||
+ | !align=left align='left' bgcolor='#CCCCFF' |Keywords | ||
+ | || | ||
+ | Adenosine Triphosphatases/chemistry; Adenosine Triphosphatases/genetics; Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Escherichia coli/genetics; Gene Expression Regulation, Bacterial; Membrane Transport Proteins/chemistry; Membrane Transport Proteins/genetics; Molecular Sequence Data; Protein Biosynthesis/physiology | ||
+ | |||
+ | |- class="tableEdit_footer" | ||
+ | |<span class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.4170.F5230d73fef6b8&page=4170&pagename={{FULLPAGENAMEE}}&type=1&template=PMID_info_table edit table]</span> || | ||
+ | |} | ||
+ | <!--box uid=d41d8cd98f00b204e9800998ecf8427e.4170.F5230d73fef6b8--> | ||
+ | |||
+ | ==Main Points of the Paper == | ||
+ | {{LitSignificance}} | ||
+ | |||
+ | == Materials and Methods Used == | ||
+ | {{LitMaterials}} | ||
+ | |||
+ | ==Phenotype Annotations== | ||
+ | {{AnnotationTableHelp}} | ||
+ | <protect><!--box uid=d41d8cd98f00b204e9800998ecf8427e.4170.G5230d740391ee--> | ||
+ | <!-- | ||
+ | ****************************************************************************************** | ||
+ | * | ||
+ | * ** 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="G5230d740391ee" 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" | ||
+ | |<span class="tableEdit_editLink plainlinks">[{{SERVER}}{{SCRIPTPATH}}?title=Special:TableEdit&id=d41d8cd98f00b204e9800998ecf8427e.4170.G5230d740391ee&page=4170&pagename={{FULLPAGENAMEE}}&type=0&template=Phenotype_Table_2 edit table]</span> || || || || || || || || || | ||
+ | |} | ||
+ | <!--box uid=d41d8cd98f00b204e9800998ecf8427e.4170.G5230d740391ee--></protect> | ||
+ | |||
+ | ==Notes== | ||
+ | |||
+ | ==References== | ||
+ | {{RefHelp}} | ||
+ | <references/> | ||
+ | |||
+ | |||
+ | [[Category:Publication]] |
Latest revision as of 15:49, 11 September 2013
Citation |
No author listed (2004) Control of SecA and SecM translation by protein secretion. Curr. Opin. Microbiol. 7:145-50 |
---|---|
Abstract |
SecA, the protein translocation ATPase of E. coli is subject to secretion-defect-response control. SecM (secretion monitor) encoded by the 5' region of the secM-secA mRNA is involved in this regulation. SecM translation is subject to transient elongation arrest at Pro166, which is prolonged when export of the nascent SecM is blocked. An "arrest sequence", FXXXXWIXXXXGIRAGP, was identified at a carboxy-terminal region of SecM that interacts with the ribosomal exit tunnel. Presumably, the stalled ribosome disrupts the secondary structure of the secM-secA mRNA such that the Shine-Dalgarno sequence for translation of secA is exposed. Mutation studies established that the SecM elongation arrest is required for the viability of E. coli as well as for constitutive (in secretion-proficient cells) and upregulated (in secretion compromised cells) expression of SecA. Furthermore, evidence suggests that elongation-arresting SecM has a role of upregulating the functionality of newly synthesized SecA molecules, presumably by bringing the mRNA to the vicinity of the membrane/Sec translocation apparatus. These results are discussed in relation to the versatile nature of SecA in its localization and structure. |
Links |
PubMed Online version:10.1016/j.mib.2004.01.001 |
Keywords |
Adenosine Triphosphatases/chemistry; Adenosine Triphosphatases/genetics; Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Escherichia coli/genetics; Gene Expression Regulation, Bacterial; Membrane Transport Proteins/chemistry; Membrane Transport Proteins/genetics; Molecular Sequence Data; Protein Biosynthesis/physiology |
edit table |
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 |
---|---|---|---|---|---|---|---|---|---|
edit table |
</protect>
Notes
References
See Help:References for how to manage references in omp dev.