Sec-independent protein translocation by the maize Hcf106 protein

Settles, A. M., Yonetani, A., Baron, A., Bush, D. R., Cline, K., Martienssen, R. (November 1997) Sec-independent protein translocation by the maize Hcf106 protein. Science, 278 (5342). pp. 1467-1470. ISSN 0036-8075

URL: http://www.ncbi.nlm.nih.gov/pubmed/9367960
DOI: 10.1126/science.278.5342.1467

Abstract

The bacterial Sec and signal recognition particle (ffh-dependent) protein translocation mechanisms are conserved between prokaryotes and higher plant chloroplasts. A third translocation mechanism in chloroplasts [the proton concentration difference (Delta pH) pathway] was previously thought to be unique. The hcf106 mutation of maize disrupts the localization of proteins transported through this Delta pH pathway in isolated chloroplasts. The Hcf106 gene encodes a receptor-like thylakoid membrane protein, which shows homology to open reading frames from all completely sequenced bacterial genomes, which suggests that the Delta pH pathway has been conserved since the endosymbiotic origin of chloroplasts. Thus, the third protein translocation pathway, of which HCF106 is a component, is found in both bacteria and plants.

Item Type: Paper
Uncontrolled Keywords: escherichia-coli thylakoid membrane signal peptide transport export pathway mutations homolog nuclear binding
Subjects: organism description > plant > maize
organism description > plant
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein translocation
CSHL Authors:
Communities: CSHL labs > Martienssen lab
Depositing User: Matt Covey
Date: November 1997
Date Deposited: 13 Dec 2013 15:29
Last Modified: 13 Dec 2013 15:29
Related URLs:
URI: http://repository.cshl.edu/id/eprint/29002

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