Sec-Independent Protein Translocation by the Maize Hcf106 Protein

See allHide authors and affiliations

Science  21 Nov 1997:
Vol. 278, Issue 5342, pp. 1467-1470
DOI: 10.1126/science.278.5342.1467

You are currently viewing the abstract.

View Full Text

Log in to view the full text

Log in through your institution

Log in through your institution


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 (ΔpH) pathway] was previously thought to be unique. Thehcf106 mutation of maize disrupts the localization of proteins transported through this ΔpH 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 ΔpH 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.

  • * 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.

View Full Text

Stay Connected to Science