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Related Concept Videos

Protein Transport to the Outer Chloroplast Membrane01:11

Protein Transport to the Outer Chloroplast Membrane

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Chloroplast outer membrane proteins encoded by the nucleus are synthesized in the cytosol. Soon after synthesis, they bind cytosolic factors such as 14-3-3 protein and the Hsp70 chaperones that keep these precursors in an unfolded state until their translocation.
Two models describe the mechanism of precursor recognition and entry across the outer membrane through the TOC complex. Model 1 suggests the newly synthesized precursor binds to the TOC receptor 159 and forms a complex.
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Protein Transport to the Inner Chloroplast Membrane01:18

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Proteins targeted to the inner chloroplast membrane, or plastid proteins, are transported by two general pathways: the stop-transfer and the re-insertion or post-import pathways. Most plastid proteins carry N-terminal transit sequences and internal import sequences targeting it to the specific chloroplast subcompartment. Proteins targeted by the stop-transfer pathway have internal hydrophobic sequences that inhibit their translocation into the stroma. As a result, these precursors are arrested...
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The Proteasome02:18

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Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
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The Proteasome01:13

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Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
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Translocation of Proteins into the Mitochondria01:19

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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
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Determining Membrane Protein Topology Using Fluorescence Protease Protection FPP
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Plastid intramembrane proteolysis.

Zach Adam1

  • 1The Robert H. Smith Institute of Plant Sciences and Genetics in Agriculture, The Hebrew University of Jerusalem, Rehovot 76100, Israel.

Biochimica Et Biophysica Acta
|December 22, 2014
PubMed
Summary

Regulated intramembrane proteolysis (RIP) in chloroplasts is crucial for plant development. Research highlights rhomboid and site-2 proteases (S2Ps) roles in fertility, chloroplast development, and gene regulation.

Area of Science:

  • Plant Biology
  • Molecular Biology
  • Cell Biology

Background:

  • Regulated intramembrane proteolysis (RIP) is vital in cellular processes, but its role in plant chloroplasts remains underexplored.
  • Limited studies have identified rhomboid proteases and site-2 proteases (S2Ps) within chloroplasts.

Purpose of the Study:

  • To review and synthesize current knowledge on RIP in plant chloroplasts.
  • To highlight the known functions and implications of chloroplast-located intramembrane proteases.

Main Methods:

  • Literature review of existing research on RIP in plant chloroplasts.
  • Analysis of mutant phenotypes associated with chloroplast proteases.

Main Results:

  • Chloroplast rhomboid proteases are linked to fertility and flower morphology, potentially via jasmonic acid biosynthesis.
Keywords:
ChloroplastProteaseRhomboid proteaseSite-2 protease

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  • Mutations in S2P homologues cause chlorophyll deficiency and impaired chloroplast development.
  • A known RIP substrate is a chloroplast envelope PHD transcription factor, releasing a domain to regulate ABA response gene ABI4 in the nucleus.

    • Conclusions:

    • Intramembrane proteases play significant roles in chloroplast biology, affecting development, gene expression, and physiological processes.
    • Further research is needed to identify specific genes and elucidate the mechanisms of these proteases and their substrates in chloroplasts.