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Related Concept Videos

Master Transcription Regulators02:23

Master Transcription Regulators

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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Cooperative Binding of Transcription Regulators

Transcriptional regulators bind to specific cis-regulatory sequences in the DNA to regulate gene transcription. These cis-regulatory sequences are very short, usually less than ten nucleotide pairs in length. The short length means that there is a high probability of the exact same sequence randomly occurring throughout the genome.  Since regulators can also bind to groups of similar sequences, this further increases the chances of random binding. Transcriptional regulators form dimers that...
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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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Nucleosome Remodeling02:54

Nucleosome Remodeling

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Sequence-specific Labeling of Nucleic Acids and Proteins with Methyltransferases and Cofactor Analogues
12:07

Sequence-specific Labeling of Nucleic Acids and Proteins with Methyltransferases and Cofactor Analogues

Published on: November 22, 2014

Long-range structural and dynamical changes induced by cofactor binding in DNA methyltransferase M.HhaI.

Hongjun Zhou1, Whitney Shatz, Matthew M Purdy

  • 1Department of Chemistry and Biochemistry, University of California, Santa Barbara, California 93106-9510, USA.

Biochemistry
|May 26, 2007
PubMed
Summary

Cofactor binding to bacterial DNA methyltransferase M.HhaI induces widespread structural changes, revealing allosteric regulation mechanisms. These dynamics influence DNA interactions, crucial for enzyme function.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Bacterial DNA cytosine methyltransferase M.HhaI modifies DNA via an S-adenosylmethionine-dependent reaction.
  • The enzyme positions target cytosine (GCGC) into an extrahelical conformation, involving active site loop movement (residues 80-99).

Purpose of the Study:

  • To characterize the structural and dynamical effects of cofactor binding on M.HhaI in solution.
  • To investigate the role of cofactor-induced dynamics in enzyme allostery and DNA interaction regulation.

Main Methods:

  • Multidimensional, transverse relaxation-optimized NMR experiments were employed.
  • Nearly 80% of residues in the cofactor-bound enzyme were assigned for structural and dynamical analysis.

Main Results:

  • Cofactor binding induced numerous structural changes across M.HhaI, including at the cofactor site and distal regions (>30 Å).
  • The active site loop exhibits picosecond-nanosecond and microsecond-millisecond dynamics, largely unaffected by cofactor binding except for N-terminal residues.
  • Cofactor binding impacts residues near the DNA binding cleft, suggesting a regulatory role.

Conclusions:

  • Cofactor binding to M.HhaI induces significant allosteric structural and dynamic changes.
  • These dynamics are closely linked to the observed allosteric properties and regulation of DNA interactions.