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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,
Kenneth Cline,
Rob Martienssen
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 ( pH) pathway] was previously thought to be unique. The
hcf106 mutation of maize disrupts the localization of
proteins transported through this 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 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.
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.
To whom correspondence should be addressed.
Read the Full Text
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157, 205-210
| Abstract »
| Full Text »
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