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Related Concept Videos

Single-Strand DNA Binding Proteins01:03

Single-Strand DNA Binding Proteins

For successful DNA replication, the unwinding of double-stranded DNA must be accompanied by stabilization and protection of the separated single strands of the DNA. This crucial task is performed by single-strand DNA-binding (SSB) proteins. They bind to the DNA in a sequence-independent manner, which means that the nitrogenous bases of the DNA need not be present in a specific order for binding of SSB proteins to it. The binding of SSB proteins straightens single-stranded DNA (ssDNA) and makes...
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Ligand Binding and Linkage00:49

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An Assay for Quantifying Protein-RNA Binding in Bacteria
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Published on: June 12, 2019

Kinky binding and SECsy insertions.

Simon J Morley1, Mark Willett

  • 1Department of Biochemistry, School of Life Sciences, University of Sussex, Brighton BN1 9QG, UK. s.j.morley@sussex.ac.uk

Molecular Cell
|September 1, 2009
PubMed
Summary
This summary is machine-generated.

Selenocysteine protein translation is regulated by the binding of eIF4a3 and SECIS binding protein 2 (SBP2) to mRNA. This interaction controls protein synthesis via a cis-acting element in the 3

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Published on: August 9, 2019

Area of Science:

  • Molecular Biology
  • Gene Expression Regulation
  • Protein Synthesis

Background:

  • Selenocysteine is an amino acid incorporated into proteins via a unique co-translational mechanism.
  • The regulation of selenocysteine incorporation is crucial for cellular function and involves specific cis-acting elements and protein factors.

Purpose of the Study:

  • To investigate the regulatory mechanism controlling the selective translation of selenocysteine-containing proteins.
  • To elucidate the roles of eIF4a3 and SECIS binding protein 2 (SBP2) in this process.

Main Methods:

  • Analysis of cis-acting elements in the 3' untranslated region (3'UTR) of target mRNAs.
  • Investigating the binding interactions of eIF4a3 and SBP2 to these elements.

Main Results:

  • Demonstrated that eIF4a3 and SBP2 bind mutually exclusively to a cis-acting element in the 3'UTR.
  • This mutually exclusive binding regulates the selective translation of selenocysteine-containing proteins.

Conclusions:

  • The study reveals a novel regulatory mechanism for selenocysteine protein synthesis.
  • The interplay between eIF4a3 and SBP2 is critical for controlling gene expression at the translational level.