7dy6: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==== | ==A refined cryo-EM structure of an Escherichia coli RNAP-promoter open complex (RPo) with SspA== | ||
<StructureSection load='7dy6' size='340' side='right'caption='[[7dy6]]' scene=''> | <StructureSection load='7dy6' size='340' side='right'caption='[[7dy6]], [[Resolution|resolution]] 3.68Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | <table><tr><td colspan='2'>[[7dy6]] is a 11 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DY6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DY6 FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7dy6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dy6 OCA], [https://pdbe.org/7dy6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dy6 RCSB], [https://www.ebi.ac.uk/pdbsum/7dy6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dy6 ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.68Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7dy6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dy6 OCA], [https://pdbe.org/7dy6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dy6 RCSB], [https://www.ebi.ac.uk/pdbsum/7dy6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dy6 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/SSPA_ECOLI SSPA_ECOLI] Forms an equimolar complex with the RNA polymerase holoenzyme (RNAP) but not with the core enzyme. It is synthesized predominantly when cells are exposed to amino acid starvation, at which time it accounts for over 50% of the total protein synthesized. It is involved in the transition from P1 early to P1 late gene expression. Rnk and SspA can functionally replace P.aeruginosa alginate regulatory gene algR2. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Stringent starvation protein A (SspA) involved in nucleotide metabolism, acid tolerance and virulence of bacteria has been demonstrated to function as a transcription factor to regulate sigma(70)-dependent gene transcription through interacting with sigma(70) region 4 and the zinc binding domain (ZBD) of E. coli RNA polymerase (EcoRNAP) beta' subunit simultaneously. Despite extensive biochemical and structural analyses were reported recently, the interactions of SspA with RNAP are not comprehensively understood. Here, we reprocessed our previous cryo-EM dataset of EcoRNAP-promoter open complex with SspA (SspA-RPo) and obtained a significantly improved density map. Unexpectedly, the new map showed that SspA interacts with both N-terminal helix of beta' subunit (beta'NuTauEta) and omega subunit, which contributes to stabilize the SspA-EcoRNAP sigma(70) holoenzyme complex. Sequence alignments and phylogenetic tree analyses of N-terminal sequences of beta' subunit from different classes of bacteria revealed that beta'NuTauEta is highly conserved and exclusively found in low-GC-content Gram-negative bacteria that harbor SspA, implying a co-evolution of beta'NuTauEta and SspA. The transcription assays of wild-type SspA and its mutants demonstrated the interaction between SspA and beta'NuTauEta facilitates the transcription regulation of SspA. Together, our results provide a more comprehensive insight into the interactions between SspA and RNAP and their roles in bacterial transcription regulation. | |||
A unique binding between SspA and RNAP beta(')NTH across low-GC Gram-negative bacteria facilitates SspA-mediated transcription regulation.,Wang F, Feng Y, Shang Z, Lin W Biochem Biophys Res Commun. 2021 Oct 27;583:86-92. doi: , 10.1016/j.bbrc.2021.10.048. PMID:34735884<ref>PMID:34735884</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7dy6" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[RNA polymerase 3D structures|RNA polymerase 3D structures]] | |||
*[[Sigma factor 3D structures|Sigma factor 3D structures]] | |||
*[[Stringent starvation protein 3D structures|Stringent starvation protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Escherichia coli]] | |||
[[Category: Escherichia coli K-12]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Lin W]] | ||
Latest revision as of 08:42, 5 June 2024
A refined cryo-EM structure of an Escherichia coli RNAP-promoter open complex (RPo) with SspAA refined cryo-EM structure of an Escherichia coli RNAP-promoter open complex (RPo) with SspA
Structural highlights
FunctionSSPA_ECOLI Forms an equimolar complex with the RNA polymerase holoenzyme (RNAP) but not with the core enzyme. It is synthesized predominantly when cells are exposed to amino acid starvation, at which time it accounts for over 50% of the total protein synthesized. It is involved in the transition from P1 early to P1 late gene expression. Rnk and SspA can functionally replace P.aeruginosa alginate regulatory gene algR2. Publication Abstract from PubMedStringent starvation protein A (SspA) involved in nucleotide metabolism, acid tolerance and virulence of bacteria has been demonstrated to function as a transcription factor to regulate sigma(70)-dependent gene transcription through interacting with sigma(70) region 4 and the zinc binding domain (ZBD) of E. coli RNA polymerase (EcoRNAP) beta' subunit simultaneously. Despite extensive biochemical and structural analyses were reported recently, the interactions of SspA with RNAP are not comprehensively understood. Here, we reprocessed our previous cryo-EM dataset of EcoRNAP-promoter open complex with SspA (SspA-RPo) and obtained a significantly improved density map. Unexpectedly, the new map showed that SspA interacts with both N-terminal helix of beta' subunit (beta'NuTauEta) and omega subunit, which contributes to stabilize the SspA-EcoRNAP sigma(70) holoenzyme complex. Sequence alignments and phylogenetic tree analyses of N-terminal sequences of beta' subunit from different classes of bacteria revealed that beta'NuTauEta is highly conserved and exclusively found in low-GC-content Gram-negative bacteria that harbor SspA, implying a co-evolution of beta'NuTauEta and SspA. The transcription assays of wild-type SspA and its mutants demonstrated the interaction between SspA and beta'NuTauEta facilitates the transcription regulation of SspA. Together, our results provide a more comprehensive insight into the interactions between SspA and RNAP and their roles in bacterial transcription regulation. A unique binding between SspA and RNAP beta(')NTH across low-GC Gram-negative bacteria facilitates SspA-mediated transcription regulation.,Wang F, Feng Y, Shang Z, Lin W Biochem Biophys Res Commun. 2021 Oct 27;583:86-92. doi: , 10.1016/j.bbrc.2021.10.048. PMID:34735884[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||