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Science 21 November 1997:
Vol. 278. no. 5342, pp. 1467 - 1470
DOI: 10.1126/science.278.5342.1467
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Reports

Sec-Independent Protein Translocation by the Maize Hcf106 Protein

A. Mark Settles, Ann Yonetani, * Aimee Baron, Daniel R. Bush, dagger Kenneth Cline, Rob Martienssen ddagger

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.

A. M. Settles, A. Yonetani, D. R. Bush, R. Martienssen, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724, USA.
A. Baron, Department of Psychiatry and Behavioral Sciences, Emory University School of Medicine, Atlanta, GA 30322, USA.
K. Cline, Department of Horticultural Sciences, University of Florida, Gainesville, FL 32611, USA.
*   Present address: Department of Biochemistry and Biophysics, University of California, San Francisco, CA 94143, USA.

dagger    Permanent address: Photosynthesis Research Unit, U.S. Department of Agriculture--Agricultural Research Service, and Department of Plant Biology, University of Illinois, Urbana, IL 61801, USA.

ddagger    To whom correspondence should be addressed.

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Science. ISSN 0036-8075 (print), 1095-9203 (online)