A Signal Peptide That Directs Non-Sec Transport in Bacteria Also Directs Efficient and Exclusive Transport on the Thylakoid Delta pH Pathway
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference17 articles.
1. IMPORT AND ROUTING OF NUCLEUS-ENCODED CHLOROPLAST PROTEINS
2. Domain structure of mitochondrial and chloroplast targeting peptides
3. A new type of signal peptide: central role of a twin-arginine motif in transfer signals for the delta pH-dependent thylakoidal protein translocase.
4. Pathway specificity for a ΔpH-dependent precursor thylakoid lumen protein is governed by a 'Sec-avoidance' motif in the transfer peptide and a 'Sec-incompatible' mature protein
5. Targeting Determinants and Proposed Evolutionary Basis for the Sec and the Delta pH Protein Transport Systems in Chloroplast Thylakoid Membranes
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1. Direct Interaction between a Precursor Mature Domain and Transport Component Tha4 during Twin Arginine Transport of Chloroplasts;Plant Physiology;2012-12-03
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3. A HupS-GFP fusion protein demonstrates a heterocyst-specific localization of the uptake hydrogenase in Nostoc punctiforme;FEMS Microbiology Letters;2011-01-24
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