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Protein Modifications in the RER01:26

Protein Modifications in the RER

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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
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Cells contain membrane-bound organelles called peroxisomes that oxidize organic molecules by transferring hydrogen atoms to oxygen, producing hydrogen peroxide. Peroxisomes enzymatically convert the released hydrogen peroxide into water and oxygen.
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ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
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Peptide Bonds

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A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
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After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
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Oxidative Peptide Backbone Cleavage by a HEXXH Enzyme During RiPP Biosynthesis.

Yao Ouyang1, Yue Yu1, Lingyang Zhu2

  • 1Department of Chemistry and Howard Hughes Medical Institute, 600 South Mathews Avenue, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA.

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Summary
This summary is machine-generated.

This study characterizes novel enzymes from Pseudomonas strains, expanding the known catalytic repertoire for bacterial RiPP biosynthesis. Researchers identified new transformations, including backbone cleavage and rare amino acid modifications.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Microbiology

Background:

  • Ribosomally synthesized and post-translationally modified peptides (RiPPs) are generated by diverse enzymes.
  • Understanding these enzymatic pathways is crucial for discovering novel bioactive compounds.

Purpose of the Study:

  • To characterize novel enzymes from two Pseudomonas biosynthetic gene clusters (BGCs).
  • To expand the known catalytic repertoire and structural diversity in RiPP biosynthesis.

Main Methods:

  • Enzyme characterization from *pfl* and *pos* BGCs.
  • Mutational analysis of enzyme active sites and recognition motifs.
  • Investigating leader peptide-enzyme interactions.

Main Results:

  • Identified two α-ketoglutarate-dependent HEXXH enzymes (PflC, PosC) catalyzing glutamine hydroxylation and backbone cleavage.
  • Discovered a unique MNIO-nitroreductase fusion enzyme installing Z-dehydrophenylalanine and hydroxylating Asp residue.
  • PflC showed proteolytic activity independent of the leader peptide, suggesting modulation of selectivity.

Conclusions:

  • This work significantly expands the catalytic capabilities and structural diversity of bacterial RiPP biosynthesis.
  • Identified key enzyme mechanisms and motifs that can be exploited for synthetic biology applications.