{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["14"],"submitter":["Avila-Castaneda A"],"pubmed_abstract":["<h4>Background</h4>NaTrxh, a thioredoxin type h, shows differential expression between self-incompatible and self-compatible Nicotiana species. NaTrxh interacts in vitro with S-RNase and co-localizes with it in the extracellular matrix of the stylar transmitting tissue. NaTrxh contains N- and C-terminal extensions, a feature shared by thioredoxin h proteins of subgroup 2. To ascertain the function of these extensions in NaTrxh secretion and protein-protein interaction, we performed a deletion analysis on NaTrxh and fused the resulting variants to GFP.<h4>Results</h4>We found an internal domain in the N-terminal extension, called Nβ, that is essential for NaTrxh secretion but is not hydrophobic, a canonical feature of a signal peptide. The lack of hydrophobicity as well as the location of t"],"journal":["BMC plant biology"],"pagination":["147"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4065587"],"repository":["biostudies-literature"],"pubmed_title":["A novel motif in the NaTrxh N-terminus promotes its secretion, whereas the C-terminus participates in its interaction with S-RNase in vitro."],"pmcid":["PMC4065587"],"pubmed_authors":["Martinez-Castilla LP","Cruz-Zamora Y","Avila-Castaneda A","Bravo-Alberto CE","Cruz-Garcia F","Rodriguez-Sotres R","Ibarra-Sanchez CP","Marquez-Guzman J","Juarez-Diaz JA","Zavala-Castillo A"],"additional_accession":[]},"is_claimable":false,"name":"A novel motif in the NaTrxh N-terminus promotes its secretion, whereas the C-terminus participates in its interaction with S-RNase in vitro.","description":"<h4>Background</h4>NaTrxh, a thioredoxin type h, shows differential expression between self-incompatible and self-compatible Nicotiana species. NaTrxh interacts in vitro with S-RNase and co-localizes with it in the extracellular matrix of the stylar transmitting tissue. NaTrxh contains N- and C-terminal extensions, a feature shared by thioredoxin h proteins of subgroup 2. To ascertain the function of these extensions in NaTrxh secretion and protein-protein interaction, we performed a deletion analysis on NaTrxh and fused the resulting variants to GFP.<h4>Results</h4>We found an internal domain in the N-terminal extension, called Nβ, that is essential for NaTrxh secretion but is not hydrophobic, a canonical feature of a signal peptide. The lack of hydrophobicity as well as the location of t","dates":{"release":"2014-01-01T00:00:00Z","publication":"2014 May","modification":"2026-04-08T03:02:41.706Z","creation":"2019-03-27T01:30:34Z"},"accession":"S-EPMC4065587","cross_references":{"pubmed":["24886483"],"doi":["10.1186/1471-2229-14-147"]}}