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Production of Pharmaceuticals01:30

Production of Pharmaceuticals

Industrial insulin production uses genetically engineered E. coli expressing a proinsulin gene controlled by a tryptophan promoter and containing a methionine linker for later cleavage. The cells also carry ampicillin resistance for selective growth. Seed cultures are stored at −80 °C and production begins by thawing a small amount to inoculate starter cultures, which are progressively scaled to a 50,000-L bioreactor. In the bioreactor, E. coli grow in nutrient-rich media under sterile, tightly...
Protein Modifications in the RER01:26

Protein Modifications in the RER

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 sequences.
tRNA Activation02:26

tRNA Activation

Aminoacyl-tRNA synthetases are present in both eukaryotes and bacteria. Though eukaryotes have 20 different aminoacyl-tRNA synthetases to couple to 20 amino acids, many bacteria do not have genes for all of these aminoacyl-tRNA synthetases. Despite this, they still use all 20 amino acids to synthesize their proteins. For instance, some bacteria do not have the gene encoding the enzyme that couples glutamine with its partner tRNA. In these organisms, one enzyme adds glutamic acid to all of the...
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
The Proteasome02:18

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...

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Video Experimental Relacionado

Updated: May 21, 2026

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation
11:09

Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation

Published on: August 1, 2018

La síntesis del tioester de proteínas habilitada por la sortaasa.

Jingjing J Ling1, Rocco L Policarpo, Amy E Rabideau

  • 1Department of Chemistry, Massachusetts Institute of Technology, 16-573a, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, USA.

Journal of the American Chemical Society
|June 13, 2012
PubMed
Resumen
Este resumen es generado por máquina.

Los investigadores desarrollaron un nuevo y sencillo método utilizando la sortasa A para crear tioesters de proteínas, cruciales para la semisíntesis de proteínas. Esta técnica facilita la ingeniería avanzada de proteínas y las estrategias de ligadura.

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Área de la Ciencia:

  • La bioquímica es la bioquímica.
  • Ingeniería de proteínas Ingeniería de proteínas.
  • Biología sintética Biología sintética.

Sus antecedentes:

  • Las proteínas con tioésteres C-terminales son intermediarios clave en la semisíntesis de proteínas.
  • Los métodos actuales para sintetizar tioesters de proteínas se basan principalmente en inteligencias de ingeniería.

Objetivo del estudio:

  • Introducir una estrategia sencilla y rutinaria para la preparación de proteínas recombinantes con (α) tioesters. terminales C.
  • Para demostrar la utilidad de este método en la síntesis de construcciones complejas de proteínas.

Principales métodos:

  • Sortasa A utilizada para la preparación de proteínas recombinantes que contienen un (α) tioestero C-terminal.
  • Aplicó el método para sintetizar dos proteínas de carga de la toxina del ántrax, una con un (α) tioester y otra con un segmento de polipéptido D.
  • Se evaluó la translocación de estas variantes a través del poro protector del antígeno.

Principales resultados:

  • Se prepararon con éxito proteínas recombinantes con (α) tioesters C-terminales utilizando la sortasa A.
  • Demostró la síntesis de una proteína que contiene un segmento de polipéptido D entre dominios.
  • Confirmó que ambas variantes de proteínas diseñadas podrían translocarse a través del poro protector del antígeno.

Conclusiones:

  • La estrategia basada en la sortasa A ofrece una alternativa simple y eficiente para la síntesis de proteína tioesters.
  • Este método permite la integración de la ligadura mediada por sortasa con la ligadura química nativa para la construcción avanzada de proteínas.
  • La técnica desarrollada amplía las posibilidades en la semisíntesis de proteínas y la ingeniería de biomoléculas complejas.