{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Rank L"],"funding":["NIAID NIH HHS","HHS | NIH | National Cancer Institute","NCI NIH HHS","HHS | NIH | National Institute of Allergy and Infectious Diseases"],"pagination":["e00685-20"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8088607"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["203(10)"],"pubmed_abstract":["Mycobacteria possess Mce transporters that import lipids and are thought to function analogously to ATP-binding cassette (ABC) transporters. However, whereas ABC transporters import substrates using a single solute-binding protein (SBP) to deliver a substrate to permease proteins in the membrane, mycobacterial Mce transporters have a potential for six SBPs (MceA to MceF) working with a pair of permeases (YrbEA and YrbEB), a cytoplasmic ATPase (MceG), and multiple Mce-associated membrane (Mam) and orphaned Mam (Omam) proteins to transport lipids. In this study, we used the model mycobacterium <i>Mycobacterium smegmatis</i> to study the requirement for individual Mce, Mam, and Omam proteins in Mce4 transport of cholesterol. All of the Mce4 and Mam4 proteins we investigated were required for "],"journal":["Journal of bacteriology"],"pubmed_title":["Evidence for the Mycobacterial Mce4 Transporter Being a Multiprotein Complex."],"pmcid":["PMC8088607"],"funding_grant_id":["P30CA016086","P30 CA016086","AI135899","R21 AI135899"],"pubmed_authors":["Braunstein M","Herring LE","Rank L"],"additional_accession":[]},"is_claimable":false,"name":"Evidence for the Mycobacterial Mce4 Transporter Being a Multiprotein Complex.","description":"Mycobacteria possess Mce transporters that import lipids and are thought to function analogously to ATP-binding cassette (ABC) transporters. However, whereas ABC transporters import substrates using a single solute-binding protein (SBP) to deliver a substrate to permease proteins in the membrane, mycobacterial Mce transporters have a potential for six SBPs (MceA to MceF) working with a pair of permeases (YrbEA and YrbEB), a cytoplasmic ATPase (MceG), and multiple Mce-associated membrane (Mam) and orphaned Mam (Omam) proteins to transport lipids. In this study, we used the model mycobacterium <i>Mycobacterium smegmatis</i> to study the requirement for individual Mce, Mam, and Omam proteins in Mce4 transport of cholesterol. All of the Mce4 and Mam4 proteins we investigated were required for ","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Apr","modification":"2026-05-08T15:54:00.203Z","creation":"2024-11-21T07:36:14.104Z"},"accession":"S-EPMC8088607","cross_references":{"pubmed":["33649150"],"doi":["10.1128/jb.00685-20","10.1128/JB.00685-20"]}}