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Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
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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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Peptide Prenylation Follows Divergent Substrate Engagement Rules.

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Prenylation of lanthipeptides involves recognizing the entire precursor peptide, including the leader region. This differs from other RiPP prenyltransferases, suggesting leader recognition dictates substrate specificity.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Natural Product Chemistry

Background:

  • Lipidation is a key modification for bioactivity in ribosomally synthesized and post-translationally modified peptides (RiPPs).
  • Lanthipeptides are a diverse class of RiPPs, and their prenylation is a critical step in their biosynthesis.

Purpose of the Study:

  • To investigate the substrate recognition mechanism of lanthipeptide prenyltransferases.
  • To compare the prenylation mechanism of lanthipeptides with that of other RiPPs, such as cyanobactins.

Main Methods:

  • Biochemical assays to study enzyme kinetics and substrate binding.
  • Bioinformatic analysis of prenyltransferase sequences and substrate interactions.

Main Results:

  • Lanthipeptide prenyltransferases recognize the complete precursor peptide, including the N-terminal leader region.
  • This leader-inclusive recognition contrasts with cyanobactin prenyltransferases, which do not engage the leader peptide.
  • Leader peptide recognition confers substrate selectivity on lanthipeptide prenyltransferases.

Conclusions:

  • The N-terminal leader region of lanthipeptide precursors plays a crucial role in substrate selectivity for prenyltransferases.
  • This mechanism of recognition differs significantly from the leader-free prenylation observed in cyanobactins, leading to distinct substrate scopes.