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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.
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Drugs exert their therapeutic effects by interacting with receptors, enzymes, or ion channels that are present throughout the human body. The strength and duration of the interaction between a drug and its target receptor are characterized by the selectivity and specificity of the drug. Selectivity refers to a drug's strong preference for its intended target over other targets. For instance, isoprenaline, a non-selective β-adrenergic agonist, interacts with both β1- and...
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The large ribosomal subunit has several important structures essential to translation. These include the peptidyl transferase center (PTC) - which is the site where the peptide bond is formed - and a large, internal, water-filled tube through which the nascent polypeptide moves. This latter structure is called the Peptide Exit Tunnel, and it begins at the PTC and spans the body of the large ribosomal subunit. During translation, as the nascent polypeptide chain is synthesized, it passes through...
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Identification of Post-translational Modifications of Plant Protein Complexes
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Specificity and selectivity in post-translational biotin addition.

Dorothy Beckett1

  • 1Department of Chemistry & Biochemistry, University of Maryland, College Park, MD 20742, U.S.A. dbeckett@umd.edu.

Biochemical Society Transactions
|November 2, 2018
PubMed
Summary
This summary is machine-generated.

Biotinylation is essential for carboxylase function. New research reveals that biotin protein ligases exhibit previously unappreciated selectivity in attaching biotin to biotin carboxyl carrier proteins, which is vital for cellular processes.

Keywords:
post-translational biotin additionsingle turnover kineticsspecificity

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Biotin is a vital cofactor for biotin-dependent carboxylases, acting as a carboxyl group carrier.
  • Post-translational attachment of biotin to biotin carboxyl carrier (BCC) proteins by biotin protein ligases is crucial for carboxylase activity.
  • Previous studies suggested limited specificity of biotinylation across different organisms.

Purpose of the Study:

  • To investigate the selectivity of biotin protein ligases in post-translational biotin addition.
  • To determine if biotinylation exhibits physiological selectivity among various carboxylase substrates.

Main Methods:

  • Utilized single turnover kinetic techniques.
  • Measured post-translational biotin addition to BCC proteins.

Main Results:

  • Demonstrated previously unappreciated selectivity in biotin addition to BCC proteins.
  • Kinetic analysis revealed specific recognition patterns by biotin protein ligases.

Conclusions:

  • Biotinylation is a more selective process than previously thought.
  • This selectivity likely plays a significant physiological role in carboxylase regulation and function.