<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Chum AP</submitter><funding>Directorate for Biological Sciences</funding><funding>National Institute of General Medical Sciences</funding><funding>NIGMS NIH HHS</funding><pagination>1340-1349</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC6566527</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>28(7)</volume><pubmed_abstract>SurA, Skp, FkpA, and DegP constitute a chaperone network that ensures biogenesis of outer membrane proteins (OMPs) in Gram-negative bacteria. Both Skp and FkpA are holdases that prevent the self-aggregation of unfolded OMPs, whereas SurA accelerates folding and DegP is a protease. None of these chaperones is essential, and we address here how functional plasticity is manifested in nine known null strains. Using a comprehensive computational model of this network termed OMPBioM, our results suggest that a threshold level of steady state holdase occupancy by chaperones is required, but the cell is agnostic to the specific holdase molecule fulfilling this function. In addition to its foldase activity, SurA moonlights as a holdase when there is no expression of Skp and FkpA. We further interro</pubmed_abstract><journal>Protein science : a publication of the Protein Society</journal><pubmed_title>Plasticity and transient binding are key ingredients of the periplasmic chaperone network.</pubmed_title><pmcid>PMC6566527</pmcid><funding_grant_id>R01GM079440</funding_grant_id><funding_grant_id>MCB1412108</funding_grant_id><pubmed_authors>Fleming KG</pubmed_authors><pubmed_authors>Shoemaker SR</pubmed_authors><pubmed_authors>Fleming PJ</pubmed_authors><pubmed_authors>Chum AP</pubmed_authors></additional><is_claimable>false</is_claimable><name>Plasticity and transient binding are key ingredients of the periplasmic chaperone network.</name><description>SurA, Skp, FkpA, and DegP constitute a chaperone network that ensures biogenesis of outer membrane proteins (OMPs) in Gram-negative bacteria. Both Skp and FkpA are holdases that prevent the self-aggregation of unfolded OMPs, whereas SurA accelerates folding and DegP is a protease. None of these chaperones is essential, and we address here how functional plasticity is manifested in nine known null strains. Using a comprehensive computational model of this network termed OMPBioM, our results suggest that a threshold level of steady state holdase occupancy by chaperones is required, but the cell is agnostic to the specific holdase molecule fulfilling this function. In addition to its foldase activity, SurA moonlights as a holdase when there is no expression of Skp and FkpA. We further interro</description><dates><release>2019-01-01T00:00:00Z</release><publication>2019 Jul</publication><modification>2025-04-05T15:20:55.224Z</modification><creation>2020-07-04T07:13:56Z</creation></dates><accession>S-EPMC6566527</accession><cross_references><pubmed>31074917</pubmed><doi>10.1002/pro.3641</doi></cross_references></HashMap>