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Post-translational Translocation of Proteins to the RER01:27

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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.
Targeting proteins to the ER
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Certain biochemical processes, such as embryonic development and cell growth regulation, depend on the repression of specific genes. DNA binding proteins known as eukaryotic transcription inhibitors regulate the repression of gene expression in eukaryotes. The presence of these inhibitors at the required location and time in the cell is triggered by the presence of hormones and additional signals from other cells.
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Transcriptional attenuation occurs when RNA transcription is prematurely terminated due to the formation of a terminator mRNA hairpin structure.  Bacteria use these hairpins to regulate the transcription process and control the synthesis of several amino acids including histidine, lysine, threonine, and phenylalanine. Transcription attenuation takes place in the non-coding regions of mRNA.
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The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
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Identification of Post-translational Modifications of Plant Protein Complexes
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Post-Translational Modification, Phase Separation, and Robust Gene Transcription.

Hari R Singh1, Yogesh B Ostwal2

  • 1Physics Department E14, Technical University Munich, 85748 Garching, Germany.

Trends in Genetics : TIG
|November 28, 2018
PubMed
Summary
This summary is machine-generated.

New insights reveal how RNA polymerase II (Pol II) transcription is regulated. A histidine-rich domain (HRD) drives elongation, while a phosphatase switch controls termination, suggesting a new regulatory paradigm.

Keywords:
P-TEFbRNA polymerase IISeb1Spt5chromatinphase separationpost-translational modificationtranscription

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Area of Science:

  • Molecular Biology
  • Gene Regulation
  • Biochemistry

Background:

  • Gene transcription by RNA polymerase II (Pol II) is a fundamental process.
  • Understanding the precise regulatory mechanisms of Pol II transcription is crucial for deciphering cellular function and disease.
  • Recent advancements have begun to illuminate the complex factors governing transcription initiation, elongation, and termination.

Purpose of the Study:

  • To summarize recent findings on the regulatory mechanisms of RNA polymerase II (Pol II)-mediated gene transcription.
  • To highlight the roles of specific protein domains and enzymatic activities in controlling transcription.
  • To propose an emerging paradigm for robust gene transcription regulation.

Main Methods:

  • Review of recent scientific literature and reports.
  • Analysis of experimental data on protein domains and enzymatic pathways involved in transcription.
  • Synthesis of findings to establish a cohesive regulatory model.

Main Results:

  • The histidine-rich domain (HRD) has been identified as a key factor that triggers phase separation, thereby promoting transcription elongation.
  • A phosphatase switch mechanism has been shown to play a critical role in promoting transcription termination.
  • These distinct mechanisms highlight a coordinated regulation of transcription progression.

Conclusions:

  • A new understanding of transcription regulation is emerging, involving distinct molecular switches for different stages of the process.
  • The interplay between phase separation (elongation) and phosphatase activity (termination) provides a framework for robust gene transcription.
  • Further research is needed to fully elucidate this emerging paradigm and its implications.