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Related Concept Videos

Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
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A gene is a stretch of DNA that serves as the blueprint for functional RNAs and proteins. Since DNA is comprised  of nucleotides and proteins are comprised of amino acids, a mediator is required to convert the information encoded in DNA into proteins. This mediator is the messenger RNA (mRNA). mRNA copies the blueprint from DNA by a process called transcription. In eukaryotes, transcription occurs in the nucleus by complementary base-pairing with the DNA template. The mRNA is then...
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Bacterial Protein Maturation01:26

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Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
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Regulation of Expression at Multiple Steps01:23

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The gene expression in cells is regulated at different stages: (i) transcription, (ii) RNA processing, (iii) RNA localization, and (iv) translation. Transcriptional regulation is mediated by regulatory proteins such as transcription factors, activators, or repressors—these control gene expression by initiating or inhibiting the transcription of genes. Once a precursor or pre-mRNA is produced, it undergoes post-transcriptional modification, including 5' capping, splicing, and the...
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Molecular Chaperones and Protein Folding03:00

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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
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Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
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Host expression system modulates recombinant Hsp70 activity through post-translational modifications.

Mauricio M Rigo1, Thiago J Borges2, Benjamin J Lang3

  • 1School of Medicine, Pontificia Universidade Catolica do Rio Grande do Sul, Av. Ipiranga, 6681, Porto Alegre Rio Grande do Sul, Zip Code: 90619-900, Brazil.

The FEBS Journal
|March 8, 2020
PubMed
Summary
This summary is machine-generated.

Recombinant heat shock proteins (Hsp70) produced in different systems exhibit distinct post-translational modifications (PTMs). These PTMs alter protein function and immunological activity, impacting cellular interactions.

Keywords:
Escherichia coliPichia pastorisDnaKHeat-shock proteinpost-translational modifications

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Area of Science:

  • Biochemistry
  • Immunology
  • Molecular Biology

Background:

  • Recombinant protein production in model organisms introduces system-specific post-translational modifications (PTMs).
  • 70-kDa heat shock proteins (Hsp70) have known intracellular chaperone functions and emerging extracellular immunomodulatory roles.
  • Conflicting reports exist regarding the inflammatory versus immunosuppressive potential of extracellular Hsp70.

Purpose of the Study:

  • To investigate if different expression systems yield recombinant Hsp70 with varying PTMs, potentially explaining divergent immunological outcomes.
  • To analyze the impact of PTMs on the structure, ATPase activity, and immunomodulatory functions of Mycobacterium tuberculosis DnaK.

Main Methods:

  • Production and purification of DnaK from Escherichia coli and Pichia pastoris.
  • Mass spectrometry analysis of DnaK preparations to identify PTMs.
  • In silico structural comparisons and in vitro functional assays, including ATPase activity and dendritic cell (DC) modulation.
  • Phosphatase treatment to assess the role of phosphorylation.

Main Results:

  • In silico analysis revealed expression system-dependent electrostatic and topographical differences in DnaK.
  • Recombinant DnaK produced in Pichia pastoris showed significantly altered ATPase activity compared to E. coli.
  • Eukaryotic system-produced DnaK demonstrated a reduced ability to downregulate MHC II and CD86 expression on murine DCs.
  • Phosphatase treatment suggested phosphorylation as a key PTM influencing these functional differences.

Conclusions:

  • Post-translational modifications are critical, expression system-dependent characteristics of recombinant Hsp70.
  • PTMs significantly impact Hsp70 interactions with ligands and subsequent functional and immunological activities.
  • Understanding PTMs is essential for interpreting the diverse biological roles of Hsp70 and for optimizing recombinant protein production.