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Related Concept Videos

Bacterial Translocation and Protein Secretion01:26

Bacterial Translocation and Protein Secretion

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Bacterial protein secretion involves translocation systems to ensure proteins reach their designated locations, including the plasma membrane, periplasm, outer membrane, or the external environment. These translocation systems are vital for bacterial physiology, supporting processes like membrane assembly, enzymatic activity in the periplasm, and interactions with the external environment. The division of labor between Sec and Tat pathways ensures efficiency in handling proteins with diverse...
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Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Related Experiment Video

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Affinity Purification of Chloroplast Translocon Protein Complexes Using the TAP Tag
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Assembling the Tat protein translocase.

Felicity Alcock1, Phillip J Stansfeld1, Hajra Basit2

  • 1Department of Biochemistry, University of Oxford, Oxford, United Kingdom.

Elife
|December 4, 2016
PubMed
Summary
This summary is machine-generated.

The twin-arginine translocation (Tat) system uses TatA, TatB, and TatC proteins to move folded proteins across membranes. This study reveals how these proteins assemble, with TatA replacing TatB during substrate transport.

Keywords:
E. coliTat protein transportbiochemistrybiophysicsmembrane proteinsequence co-evolutionstructural biologytwin-arginine

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • The twin-arginine translocation (Tat) system is crucial for transporting folded proteins across biological membranes in bacteria and chloroplasts.
  • The Tat transporter complex is composed of membrane proteins TatA, TatB, and TatC.

Purpose of the Study:

  • To elucidate the molecular-level interactions and assembly of the Tat protein complex in *Escherichia coli*.
  • To define the structural basis of Tat transporter function.

Main Methods:

  • Sequence co-evolution analysis
  • Molecular simulations
  • Experimental validation

Main Results:

  • The TatBC receptor complex features TatB transmembrane helices sandwiched between TatC molecules.
  • A functionally important polar residue cluster mediates interactions within the TatBC complex.
  • TatA was unexpectedly found to associate with TatC at this polar cluster site.
  • A structural model suggests TatA replaces TatB at the polar cluster upon substrate binding, triggering translocase activation.

Conclusions:

  • Co-evolution analysis is a powerful tool for predicting protein-protein interactions in multi-subunit complexes.
  • The study provides a novel structural model for the assembly and activation mechanism of the Tat translocase.