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Related Concept Videos

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
Ribosome profiling has many applications, including in vivo monitoring of translation inside a particular organ or tissue type and quantifying new protein synthesis levels.
The technique...
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Profiling of Methyltransferases and Other S-adenosyl-L-homocysteine-binding Proteins by Capture Compound Mass Spectrometry CCMS
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An effective method for profiling the selenium-binding proteins using its reactive metabolic intermediate.

Eriko Hori1, Sakura Yoshida, Mamoru Haratake

  • 1Graduate School of Biomedical Sciences, Nagasaki University, 1-14 Bunkyo-machi, Nagasaki, 852-8521, Japan.

Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry
|April 22, 2015
PubMed
Summary

Researchers identified selenium-binding proteins in rat liver using a novel profiling method. This study advances understanding of selenium metabolism and its interactions with proteins like liver fatty acid-binding protein.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Toxicology

Background:

  • Intracellular selenium reduction and transport mechanisms remain largely unknown.
  • Reduced selenium species are implicated in reactions with endogenous molecules, especially thiol-containing proteins.

Purpose of the Study:

  • To develop and apply a method for identifying selenium-binding proteins in biological systems.
  • To investigate the reactivity of a selenium metabolic intermediate, L-penicillamine selenotrisulfide (PenSSeSPen), with cellular proteins.

Main Methods:

  • Utilized a profiling method involving L-penicillamine selenotrisulfide (PenSSeSPen) on rat liver cell lysate.
  • Employed MALDI TOF-MS analysis to detect thiol-exchange reactions between PenSSeSPen and cysteine residues.
  • Performed rat protein database searches and tryptic fragmentation experiments for protein identification.

Main Results:

  • Identified several cysteine-containing proteins reactive with PenSSeSPen in rat liver cell lysate.
  • The most prominent identified protein was liver fatty acid-binding protein (m/z 14,313) through thiol-exchange reactions.
  • Validated protein identification using database searches and fragmentation analysis.

Conclusions:

  • The developed methodology is effective for identifying selenium-binding proteins and selenium-interactive species.
  • This approach enhances understanding of selenium metabolism, utilization, and protein interactions within biological systems.
  • Liver fatty acid-binding protein is a significant selenium-interactive protein in rat liver cells.