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Literature DB >> 7973633

SecA homolog in protein transport within chloroplasts: evidence for endosymbiont-derived sorting.

Abstract

The SecA protein is an essential, azide-sensitive component of the bacterial protein translocation machinery. A SecA protein homolog (CPSecA) now identified in pea chloroplasts was purified to homogeneity. CPSecA supported protein transport into thylakoids, the chloroplast internal membrane network, in an azide-sensitive fashion. Only one of three pathways for protein transport into thylakoids uses the CPSecA mechanism. The use of a bacteria-homologous mechanism in intrachloroplast protein transport provides evidence for conservative sorting of proteins within chloroplasts.

Entities: Chemical

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Year: 1994 PMID： 7973633 DOI： 10.1126/science.7973633

Source DB: PubMed Journal: Science ISSN： 0036-8075 Impact factor: 47.728

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Cited

46 in total

1. Arabidopsis mutants lacking the 43- and 54-kilodalton subunits of the chloroplast signal recognition particle have distinct phenotypes.

Authors: P Amin; D A Sy; M L Pilgrim; D H Parry; L Nussaume; N E Hoffman
Journal: Plant Physiol Date: 1999-09 Impact factor: 8.340

2. Interaction of a plant 14-3-3 protein with the signal peptide of a thylakoid-targeted chloroplast precursor protein and the presence of 14-3-3 isoforms in the chloroplast stroma.

Authors: P C Sehnke; R Henry; K Cline; R J Ferl
Journal: Plant Physiol Date: 2000-01 Impact factor: 8.340

3. Differential dependence of levansucrase and alpha-amylase secretion on SecA (Div) during the exponential phase of growth of Bacillus subtilis.

Authors: L Leloup; A J Driessen; R Freudl; R Chambert; M F Petit-Glatron
Journal: J Bacteriol Date: 1999-03 Impact factor: 3.490

8. Red bell pepper chromoplasts exhibit in vitro import competency and membrane targeting of passenger proteins from the thylakoidal sec and DeltapH pathways but not the chloroplast signal recognition particle pathway.

Authors: E J Summer; K Cline
Journal: Plant Physiol Date: 1999-02 Impact factor: 8.340

Review 9. Multiple pathways for the targeting of thylakoid proteins in chloroplasts.

Authors: C Robinson; P J Hynds; D Robinson; A Mant
Journal: Plant Mol Biol Date: 1998-09 Impact factor: 4.076

10. Analysis of the Import of Carboxyl-Terminal Truncations of the 23-Kilodalton Subunit of the Oxygen-Evolving Complex Suggests That Its Structure Is an Important Determinant for Thylakoid Transport.

Authors: R. A. Roffey; S. M. Theg
Journal: Plant Physiol Date: 1996-08 Impact factor: 8.340

SecA homolog in protein transport within chloroplasts: evidence for endosymbiont-derived sorting.

1. Arabidopsis mutants lacking the 43- and 54-kilodalton subunits of the chloroplast signal recognition particle have distinct phenotypes.

2. Interaction of a plant 14-3-3 protein with the signal peptide of a thylakoid-targeted chloroplast precursor protein and the presence of 14-3-3 isoforms in the chloroplast stroma.

3. Differential dependence of levansucrase and alpha-amylase secretion on SecA (Div) during the exponential phase of growth of Bacillus subtilis.

Review 4. Protein import and routing systems of chloroplasts.

5. Chloroplast SecA and Escherichia coli SecA have distinct lipid and signal peptide preferences.

6. On the mode of integration of plastid-encoded components of the cytochrome bf complex into thylakoid membranes.

7. Assembly of the chlorophyll-protein complexes.

8. Red bell pepper chromoplasts exhibit in vitro import competency and membrane targeting of passenger proteins from the thylakoidal sec and DeltapH pathways but not the chloroplast signal recognition particle pathway.

Review 9. Multiple pathways for the targeting of thylakoid proteins in chloroplasts.

10. Analysis of the Import of Carboxyl-Terminal Truncations of the 23-Kilodalton Subunit of the Oxygen-Evolving Complex Suggests That Its Structure Is an Important Determinant for Thylakoid Transport.