作者: Macie B. Walker , Laura M. Roy , Eric Coleman , Rodger Voelker , Alice Barkan
关键词: Chloroplast thylakoid membrane 、 Biology 、 Transmembrane protein 、 Gene product 、 Transport protein 、 Peptide sequence 、 Membrane protein 、 Thylakoid 、 Gene 、 Biochemistry
摘要: Proteins are translocated across the chloroplast thylakoid membrane by a variety of mechanisms. Some proteins engage translocation machinery that is derived from bacterial Sec export system and require an interaction with chloroplast-localized SecA homologue. Other SecA-independent, but requires transmembrane pH gradient. Recently, counterpart to this Δ mechanism was discovered in bacteria. Genetic studies revealed one maize protein involved mechanism, HCF106, related both structure function tatA tatB gene products. We describe here mutant phenotype molecular cloning second functions mechanism. This gene, assembly 4 (tha4), required specifically for pathway. The sequence tha4 product resembles those hcf106 genes. Sequence comparisons suggest more closely tatA, tatB. These findings support notion sec-independent has been highly conserved during evolution eucaryotic organelles endosymbionts.