biostudies-literatureUnknown14Avila-Castaneda A<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 tBMC plant biology147https://www.ebi.ac.uk/biostudies/studies/S-EPMC4065587biostudies-literatureA novel motif in the NaTrxh N-terminus promotes its secretion, whereas the C-terminus participates in its interaction with S-RNase in vitro.PMC4065587Martinez-Castilla LPCruz-Zamora YAvila-Castaneda ABravo-Alberto CECruz-Garcia FRodriguez-Sotres RIbarra-Sanchez CPMarquez-Guzman JJuarez-Diaz JAZavala-Castillo AfalseA novel motif in the NaTrxh N-terminus promotes its secretion, whereas the C-terminus participates in its interaction with S-RNase in vitro.<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 t2014-01-01T00:00:00Z2014 May2026-04-08T03:02:41.706Z2019-03-27T01:30:34ZS-EPMC40655872488648310.1186/1471-2229-14-147