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Related Concept Videos

Master Transcription Regulators02:23

Master Transcription Regulators

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Master transcription regulators are regulatory proteins that are predominantly responsible for regulating the expression of multiple genes. Often these genes work in concert to drive a  complex process. Activation of a master transcription regulator can lead to a cascade of transcriptional activation necessary for that outcome. These regulators can directly bind to the regulatory sequences of the various genes involved, or they can indirectly regulate transcription by binding to regulatory...
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Controlled current coulometry, also known as amperostatic coulometry, is a technique used in electrochemical analysis to measure the quantity of a substance through the controlled passage of current. It involves the application of a constant current to an electrochemical cell containing the analyte of interest. As the current flows through the cell, the analyte undergoes a redox reaction at the electrode surface, resulting in a charge transfer. By monitoring the time required for a certain...
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Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
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Calcium is an essential signaling molecule required for various cellular functions. Calcium pumps and ion channels on cell and organellar membranes, such as those on the endoplasmic reticulum (ER), regulate calcium concentrations inside the cell. They remain closed, keeping the cytosolic calcium levels low at a resting state.
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ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
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The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
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Related Experiment Video

Updated: Jun 22, 2025

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The Copper Efflux Regulator (CueR).

Yangbo Hu1, Bin Liu2

  • 1State Key Laboratory of Virology, Wuhan Institute of Virology, Center for Biosafety Mega-Science, Chinese Academy of Sciences, Wuhan, China. ybhu@wh.iov.cn.

Sub-Cellular Biochemistry
|July 4, 2024
PubMed
Summary

The copper efflux regulator (CueR) controls gene transcription for copper balance in bacteria. Copper binding causes CueR to change shape, activating genes essential for cell survival.

Keywords:
Allosteric activationCopper homeostasisMetalloregulatorPromoterRNA polymeraseTranscriptional regulation

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • The copper efflux regulator (CueR) is a MerR family metalloregulator found in gram-negative bacteria.
  • CueR regulates genes involved in copper homeostasis, crucial for cellular survival.

Purpose of the Study:

  • To review the regulatory roles and mechanisms of CueR in Escherichia coli.
  • To elucidate the molecular details of copper binding, DNA recognition, and transcriptional regulation by CueR.

Main Methods:

  • Biochemical analyses
  • Structural analyses

Main Results:

  • Detailed molecular mechanisms of CueR's transcriptional regulation.
  • CueR represses transcription without copper; copper binding induces conformational change to activate transcription.
  • Identification of functional domains and key residues involved in CueR's mechanism.

Conclusions:

  • Understanding CueR's mechanism provides insights into other MerR family metalloregulators.
  • Elucidating CueR function aids in understanding broader metalloregulator roles in organisms.