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Related Concept Videos

Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
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Protein Modifications in the RER01:26

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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.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
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Protein Glycosylation01:25

Protein Glycosylation

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Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
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Post-translational Translocation of Proteins to the RER01:27

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A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
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Pre-mRNA Processing: Modification of pre-mRNA Ends01:35

Pre-mRNA Processing: Modification of pre-mRNA Ends

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In eukaryotic cells, transcripts made by RNA polymerase are modified and processed before exiting the nucleus. Unprocessed RNA is called precursor mRNA or pre-mRNA to distinguish it from mature mRNA.
Once about 20-40 ribonucleotides have been joined together by RNA polymerase, a group of enzymes adds a cap to the 5' end of the growing transcript. In this process, a 5' phosphate is replaced by modified guanosine that has a methyl group attached (7-methyl guanosine). This 5' cap helps...
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Ribosome Profiling02:24

Ribosome Profiling

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Ribosome profiling or ribo-sequencing is a deep sequencing technique that produces a snapshot of active translation in a cell. It selectively sequences the mRNAs protected by ribosomes to get an insight into a cell’s translation landscape at any given point in time.
Applications of ribosome profiling
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A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes
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A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes

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Global Post-Translational Modification Discovery.

Qiyao Li1, Michael R Shortreed1, Craig D Wenger

  • 1Department of Chemistry, University of Wisconsin , 1101 University Avenue, Madison, Wisconsin 53706, United States.

Journal of Proteome Research
|March 2, 2017
PubMed
Summary
This summary is machine-generated.

A new global post-translational modification discovery (G-PTM-D) strategy enhances proteomics by identifying novel PTMs. This method uses a two-round mass spectrometry search for deep, high-confidence modification analysis in complex samples.

Keywords:
G-PTM-Ddatabase searchpost-translational modification discoveryproteomics

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Area of Science:

  • Proteomics
  • Biochemistry
  • Mass Spectrometry

Background:

  • Post-translational modifications (PTMs) are crucial for protein function and cellular regulation.
  • Discovering novel PTMs is essential for understanding complex biological systems.
  • Existing methods have limitations in identifying a wide range of PTMs in complex samples.

Purpose of the Study:

  • To introduce and validate a novel global post-translational modification discovery strategy (G-PTM-D).
  • To improve the depth and confidence of PTM identification in proteomics research.
  • To provide a powerful new capability for the proteomics community.

Main Methods:

  • Development of the G-PTM-D strategy, an advancement over the G-PTM strategy.
  • Utilizing a two-round mass spectrometry data search approach.
  • Supplementing a proteomics database with newly discovered PTMs from an initial wide-tolerance search.

Main Results:

  • Achieved deep coverage and identification of a rich variety of peptide modifications.
  • High confidence in PTM identification, even in complex, unenriched samples.
  • Demonstrated significant improvements over previous PTM discovery methods.

Conclusions:

  • The G-PTM-D strategy is a major advancement in PTM discovery.
  • This method offers a powerful new capability for identifying novel PTMs.
  • The strategy enables high-confidence analysis of PTMs in complex biological samples.