Insertion of PsaK into the Thylakoid Membrane in a “Horseshoe” Conformation Occurs in the Absence of Signal Recognition Particle, Nucleoside Triphosphates, or Functional Albino3-Reference-Cited by-同舟云学术

Insertion of PsaK into the Thylakoid Membrane in a “Horseshoe” Conformation Occurs in the Absence of Signal Recognition Particle, Nucleoside Triphosphates, or Functional Albino3

Published:2001-09 Issue:39 Volume:276 Page:36200-36206
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Mant Alexandra,Woolhead Cheryl A.,Moore Misty,Henry Ralph,Robinson Colin

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference33 articles.

1. Evolutionarily Related Insertion Pathways of Bacterial, Mitochondrial, and Thylakoid Membrane Proteins

2. Assembly of a cytoplasmic membrane protein inEscherichia coliis dependent on the signal recognition particle

3. The Tsr chemosensory transducer of Escherichia coli assembles into the cytoplasmic membrane via a SecA-dependent process.

4. Insertion of the Polytopic Membrane Protein MalF Is Dependent on the Bacterial Secretion Machinery

5. The Functional Integration of a Polytopic Membrane Protein of Escherichia coli is Dependent on the Bacterial Signal-Recognition Particle

Cited by 50 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. The role of chloroplast SRP54 domains and its C-terminal tail region in post- and co-translational protein transport in vivo;Journal of Experimental Botany;2024-07-11

2. A deletion in a photosynthesis-related gene (PpPSAK) determines the anthocyanin accumulation in the mesocarp of French blood-flesh peaches;2024-07-10

3. Structure, function, and assembly of PSI in thylakoid membranes of vascular plants;The Plant Cell;2024-06-07

4. The role of chloroplast SRP54 domains and its C-terminal tail region in post- and cotranslational protein transportin vivo;2024-04-22

5. Stepwise protein targeting into plastoglobules are facilitated by three hydrophobic regions of rice phytoene synthase 2;Frontiers in Plant Science;2023-05-31