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Related Concept Videos

Signal Sequences and Sorting Receptors01:41

Signal Sequences and Sorting Receptors

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Signal sequences are short amino acid sequences that guide newly synthesized proteins to their proper location within the cell. Classical signal sequences are fifteen to sixty amino acids long and present at the N-terminus of a polypeptide chain. Each signal sequence has a conserved segment of basic residues towards their N terminus, a hydrophobic core, and a C-terminus rich in polar residues. The C-terminus also contains a signal cleavage site and features a -3 -1 sequence motif. The -3-1...
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Overview of Protein Sorting and Transport01:45

Overview of Protein Sorting and Transport

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Eukaryotic cells have different membrane-bound organelles with distinct protein requirements. The process by which proteins are targeted to a specific organelle is called protein sorting.
Protein sorting can be of two types: signal-based sorting and vesicle-based trafficking. In signal-based sorting, specific amino acid sequences called sorting signals target proteins to the proper location inside the cell either via gated transport or by protein translocation.  In gated transport, folded...
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Bacterial Translocation and Protein Secretion01:26

Bacterial Translocation and Protein Secretion

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Bacterial protein secretion involves translocation systems to ensure proteins reach their designated locations, including the plasma membrane, periplasm, outer membrane, or the external environment. These translocation systems are vital for bacterial physiology, supporting processes like membrane assembly, enzymatic activity in the periplasm, and interactions with the external environment. The division of labor between Sec and Tat pathways ensures efficiency in handling proteins with diverse...
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Role of ER in the Secretory Pathway01:17

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Eukaryotic cells have a special pathway that enables communication between various intracellular membrane-bound compartments and also with the extracellular environment. This pathway is termed as the secretory pathway.
Components of the secretory pathway
About a third of proteins synthesized in the cell are sorted via the secretory route. They shuffle between different compartments in membrane-bound vesicles until they reach their final destination. The main intracellular compartments involved...
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Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

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The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
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Insertion of Single-pass Transmembrane Proteins in the RER01:26

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Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
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Related Experiment Video

Updated: Apr 27, 2026

Using SecM Arrest Sequence as a Tool to Isolate Ribosome Bound Polypeptides
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Secretion of circular proteins using sortase.

Karin Strijbis1, Hidde L Ploegh

  • 1Department of Infectious Diseases & Immunology, Utrecht University, Utrecht, The Netherlands.

Methods in Molecular Biology (Clifton, N.J.)
|June 21, 2014
PubMed
Summary

Researchers engineered circular proteins using bacterial sortase A (SrtA) enzyme. This method allows cells to secrete these circularized proteins, offering enhanced stability and activity for various applications.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Engineering

Background:

  • Circular proteins naturally exist in various organisms and are crucial for host defense.
  • These proteins exhibit superior properties like enhanced protease resistance, thermostability, and longevity.
  • Conventional linear proteins can be engineered into circular forms to harness these benefits.

Purpose of the Study:

  • To develop a method for producing engineered circular proteins within cells.
  • To leverage sortase A (SrtA) enzymatic activity for protein circularization.
  • To enable the secretion of circularized proteins from host cells.

Main Methods:

  • Utilized bacterial sortase A (SrtA) transpeptidase for enzymatic ligation of protein N- and C-termini.
  • Engineered substrate proteins designed for sortase-mediated circularization.

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  • Manipulated cellular machinery, specifically the endoplasmic reticulum lumen, for in vivo circularization and secretion.

    • Main Results:

    • Successfully demonstrated sortase-mediated circularization of engineered proteins.
    • Achieved secretion of circularized proteins from manipulated cells.
    • Established a novel in vivo method for producing circular proteins.

    Conclusions:

    • Sortase-mediated circularization is an effective strategy for creating proteins with enhanced properties.
    • This approach enables the intracellular production and secretion of engineered circular proteins.
    • The method holds potential for applications requiring stable and active protein therapeutics or enzymes.