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Related Concept Videos

Directing Proteins to the Rough Endoplasmic Reticulum01:34

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The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
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Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
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Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.
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Once a transport vesicle has recognized its target organelle, the vesicular membrane needs to fuse with the target membrane to unload the cargo. Transmembrane proteins called SNAREs present on organelle membranes and their vesicles, mediate vesicle fusion.
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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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The exosome-binding factors Rrp6 and Rrp47 form a composite surface for recruiting the Mtr4 helicase.

Benjamin Schuch1, Monika Feigenbutz2, Debora L Makino1

  • 1Structural Cell Biology Department, Max Planck Institute of Biochemistry, Martinsried, Germany.

The EMBO Journal
|October 17, 2014
PubMed
Summary

The yeast exosome complex (Exo-10) interacts with RNA processing factors Rrp6, Rrp47, and Mtr4. Structural analysis reveals Rrp6 and Rrp47 form a unit that binds Mtr4, crucial for exosome function.

Keywords:
RNA degradationX‐ray crystallographynuclear exosomeyeast genetics

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Structural Biology

Background:

  • The exosome is a vital multi-subunit ribonuclease complex.
  • It plays a key role in RNA processing, turnover, and surveillance in both nuclear and cytoplasmic compartments.
  • In the yeast nucleus, the core exosome (Exo-10) interacts with several cofactors, including Rrp6, Rrp47, Mtr4, and Mpp6.

Purpose of the Study:

  • To elucidate the structural basis of interactions between the yeast nuclear exosome core complex and its associated factors.
  • To understand the specific roles of Rrp6, Rrp47, and Mtr4 in exosome function.
  • To provide detailed structural insights into the exosome-cofactor complex.

Main Methods:

  • In vitro binding assays to study protein interactions.
  • Crystallographic analysis to determine the three-dimensional structure of protein complexes.
  • Site-directed mutagenesis to investigate the functional significance of specific residues.
  • Growth assays in yeast strains.

Main Results:

  • Mtr4 binding to Exo-10 is dependent on the presence of both Rrp6 and Rrp47.
  • Mpp6 binds directly to the exosome, independent of other cofactors.
  • Crystallography revealed that Rrp6 and Rrp47 form an intertwined structural unit.
  • This Rrp6-Rrp47 unit creates a binding groove for the N-terminus of Mtr4.
  • Mutations at the Rrp6-Mtr4 interface disrupt their interaction and impair cell growth.

Conclusions:

  • The Rrp6-Rrp47 complex acts as a crucial intermediary for Mtr4 binding to the core exosome.
  • Detailed structural insights reveal a conserved interaction surface between Rrp6-Rrp47 and Mtr4.
  • This study highlights a critical link between Mtr4 and the core exosome, essential for its nuclear functions.