{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Rodrigues RA"],"funding":["NIGMS NIH HHS"],"pagination":["600-9"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3107010"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["65(4)"],"pubmed_abstract":["The Arabidopsis thylakoid FtsH protease complex is composed of FtsH1/FtsH5 (type A) and FtsH2/FtsH8 (type B) subunits. Type A and type B subunits display a high degree of sequence identity throughout their mature domains, but no similarity in their amino-terminal targeting peptide regions. In chloroplast import assays, FtsH2 and FtsH5 were imported and subsequently integrated into thylakoids by a two-step processing mechanism that resulted in an amino-proximal lumenal domain, a single transmembrane anchor, and a carboxyl proximal stromal domain. FtsH2 integration into washed thylakoids was entirely dependent on the proton gradient, whereas FtsH5 integration was dependent on NTPs, suggesting their integration by Tat and Sec pathways, respectively. This finding was corroborated by in organel"],"journal":["The Plant journal : for cell and molecular biology"],"pubmed_title":["FtsH2 and FtsH5: two homologous subunits use different integration mechanisms leading to the same thylakoid multimeric complex."],"pmcid":["PMC3107010"],"funding_grant_id":["R01 GM046951","R01 GM46951","R01 GM046951-19"],"pubmed_authors":["Silva-Filho MC","Rodrigues RA","Cline K"],"additional_accession":[]},"is_claimable":false,"name":"FtsH2 and FtsH5: two homologous subunits use different integration mechanisms leading to the same thylakoid multimeric complex.","description":"The Arabidopsis thylakoid FtsH protease complex is composed of FtsH1/FtsH5 (type A) and FtsH2/FtsH8 (type B) subunits. Type A and type B subunits display a high degree of sequence identity throughout their mature domains, but no similarity in their amino-terminal targeting peptide regions. In chloroplast import assays, FtsH2 and FtsH5 were imported and subsequently integrated into thylakoids by a two-step processing mechanism that resulted in an amino-proximal lumenal domain, a single transmembrane anchor, and a carboxyl proximal stromal domain. FtsH2 integration into washed thylakoids was entirely dependent on the proton gradient, whereas FtsH5 integration was dependent on NTPs, suggesting their integration by Tat and Sec pathways, respectively. This finding was corroborated by in organel","dates":{"release":"2011-01-01T00:00:00Z","publication":"2011 Feb","modification":"2025-04-04T07:35:51.286Z","creation":"2019-03-27T00:42:13Z"},"accession":"S-EPMC3107010","cross_references":{"pubmed":["21214651"],"doi":["10.1111/j.1365-313x.2010.04448.x","10.1111/j.1365-313X.2010.04448.x"]}}