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Related Concept Videos

Prokaryotic Transcriptional Activators and Repressors01:58

Prokaryotic Transcriptional Activators and Repressors

The organization of prokaryotic genes in their genome is notably different from that of eukaryotes. Prokaryotic genes are organized, such that the genes for proteins involved in the same biochemical process or function are located together in groups. This group of genes, along with their regulatory elements, are collectively known as an operon. The functional genes in an operon are transcribed together to give a single strand of mRNA known as polycistronic mRNA.
Transcription of prokaryotic...
Prokaryotic Transcriptional Activators and Repressors01:58

Prokaryotic Transcriptional Activators and Repressors

The organization of prokaryotic genes in their genome is notably different from that of eukaryotes. Prokaryotic genes are organized, such that the genes for proteins involved in the same biochemical process or function are located together in groups. This group of genes, along with their regulatory elements, are collectively known as an operon. The functional genes in an operon are transcribed together to give a single strand of mRNA known as polycistronic mRNA.
Transcription of prokaryotic...
Co-activators and Co-repressors02:04

Co-activators and Co-repressors

Gene transcription is regulated by the synergistic action of several proteins that form a complex at a gene regulatory site. This is observed in eukaryotes, where the regulation of gene expression is a complex process. Regulatory proteins in eukaryotes can broadly be classified into two types – regulators that bind directly to specific DNA sequences and co-regulators that associate with regulatory proteins but cannot directly bind to the DNA. These co-regulators are further divided into...
Co-activators and Co-repressors02:04

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Gene transcription is regulated by the synergistic action of several proteins that form a complex at a gene regulatory site. This is observed in eukaryotes, where the regulation of gene expression is a complex process. Regulatory proteins in eukaryotes can broadly be classified into two types – regulators that bind directly to specific DNA sequences and co-regulators that associate with regulatory proteins but cannot directly bind to the DNA. These co-regulators are further divided into...
Repressible Operon: trp Operon01:21

Repressible Operon: trp Operon

The trp operon in Escherichia coli exemplifies a repressible operon. It regulates the synthesis of tryptophan through repressor-mediated transcriptional control and attenuation. This dual regulatory mechanism ensures tryptophan biosynthesis occurs only when needed, conserving cellular resources.Structure of the trp OperonThe trp operon consists of five structural genes (trpE, trpD, trpC, trpB, and trpA) that encode enzymes for tryptophan biosynthesis. These genes are transcribed as a single...
Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze the...

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Inducible and Reversible Dominant-negative (DN) Protein Inhibition
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Activating PER repressor through a DBT-directed phosphorylation switch.

Saul Kivimäe1, Lino Saez, Michael W Young

  • 1Laboratory of Genetics, The Rockefeller University, New York, New York, USA.

Plos Biology
|August 1, 2008
PubMed
Summary

The protein kinase Doubletime (DBT) directly phosphorylates the Period (PER) protein, a key component of the Drosophila biological clock. This phosphorylation regulates PER stability and repressor function, influencing circadian rhythmicity.

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Area of Science:

  • Chronobiology
  • Molecular biology
  • Biochemistry

Background:

  • Protein phosphorylation is crucial for circadian rhythms, affecting clock protein stability, activity, and localization.
  • The Doubletime (DBT) protein kinase is a Drosophila ortholog of human casein kinase I (CKI)epsilon/delta.

Purpose of the Study:

  • To investigate the role of DBT in phosphorylating the Drosophila clock protein Period (PER).
  • To identify DBT-dependent phosphorylation sites on PER and assess their functional significance.

Main Methods:

  • Enzymatic assays to confirm DBT's direct phosphorylation of PER.
  • Identification of PER phosphorylation sites.
  • Functional assessment in cultured cell systems and in vivo.
  • Analysis of the per(S) mutation's effect on PER phosphorylation.

Main Results:

  • DBT directly phosphorylates the Drosophila PER protein.
  • Specific DBT-dependent phosphorylation sites within PER were identified.
  • The per(S) mutation, linked to short circadian rhythms, affects a critical PER phosphorylation site.
  • Multiple DBT phosphorylations on adjacent motifs regulate PER stability and repressor function in a switch-like manner.

Conclusions:

  • DBT-mediated phosphorylation of PER is a key regulatory mechanism in Drosophila circadian rhythms.
  • Integrated phosphorylations on PER control its stability and function as a repressor.
  • Understanding these molecular mechanisms provides insight into circadian clock regulation.