The DOI matches its Crossref record; 28 of the 28 references it cites were found in a registry or an index.
Sec-Independent Protein Translocation by the Maize Hcf106 Protein
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 (ΔpH) pathway] was previously thought to be unique. The hcf106 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.
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Basic local alignment search tool
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A common export pathway for proteins binding complex redox cofactors?
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Cited by
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Bachmann, J., Bauer, B., Zwicker, K., Ludwig, B., & Anderka, O. (2006) · The FEBS Journal · doi:10.1111/j.1742-4658.2006.05480.x · Cited by 306
de Gier (1998) · doi:10.1093/emboj/18.11.2982 · Cited by 277
Metadata
- Authors
- Settles, A. M., Yonetani, A., Baron, A., Bush, D. R., Cline, K., & Martienssen, R.
- Venue
- Science
- Published
- 1997-11-21
- Volume
- 278
- Issue
- 5342
- Pages
- 1467-1470
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2136767810
- Cited by
- 286
- References
- 28
- FWCI
- 8.21
- Type
- journal article
- Language
- en
- Open access
- closed
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