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Related Concept Videos

Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

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.
Most of the mitochondrial precursors...
Proteomics01:33

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Bacterial Protein Maturation01:26

Bacterial Protein Maturation

Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
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Protein Networks02:26

Protein Networks

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JUMPn: A Streamlined Application for Protein Co-Expression Clustering and Network Analysis in Proteomics
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Published on: October 19, 2021

N-terminal protein processing: a comparative proteogenomic analysis.

Stefano Bonissone1, Nitin Gupta, Margaret Romine

  • 1Bioinformatics Program, University of California San Diego, La Jolla, California, USA. sbonisso@ucsd.edu

Molecular & Cellular Proteomics : MCP
|September 25, 2012
PubMed
Summary
This summary is machine-generated.

N-terminal methionine excision (NME) and N-terminal acetylation (NTA) are common protein modifications. This study reveals NME may primarily expose alanine and serine, and NTA is more common in prokaryotes than previously thought.

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Area of Science:

  • Proteomics
  • Post-translational Modifications
  • Comparative Genomics

Background:

  • N-terminal methionine excision (NME) and N-terminal acetylation (NTA) are prevalent protein post-translational modifications.
  • NME is a conserved mechanism, while NTA is common in eukaryotes and rare in prokaryotes.
  • Previous understanding of NME specificity and function may be incomplete.

Purpose of the Study:

  • To re-evaluate the specificity and functional roles of NME using large-scale proteogenomic data.
  • To investigate the prevalence of NTA in prokaryotes.
  • To compare NME and NTA across different life forms.

Main Methods:

  • Analysis of large proteogenomic datasets from yeast, mammals, and bacteria (112 million spectra from 57 species).
  • Comparative genomic analysis of NME substrate proteins.
  • Proteomic analysis to assess NTA prevalence in prokaryotes.

Main Results:

  • NME specificity, while generally conserved, shows modest variation in some organisms.
  • NME appears to primarily expose alanine and serine at the N-terminus, rather than all seven previously identified residues.
  • NTA is more prevalent in certain prokaryotes than previously recognized.
  • The functional significance of exposing specific N-terminal residues like alanine and serine may be linked to NTA or other modifications.

Conclusions:

  • The functional importance of NME may be narrower than previously assumed, focusing on exposing specific amino acids.
  • The prevalence of NTA in prokaryotes warrants further investigation.
  • This study provides a comprehensive proteogenomic perspective on NME and NTA.