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Related Concept Videos

DNA Helicases00:55

DNA Helicases

DNA unwinding helicase enzymes are a type of motor protein. Motor proteins can translocate along filaments or polymers using energy generated from ATP hydrolysis. Helicases are involved in all the important cellular processes where DNA unwinding is required, such as DNA replication, repair, recombination, and transcription. They are present in all living organisms, but vary in their structure, function, and mechanism of action. For example, in prokaryotes, DnaB helicase binds and translocates...
Single-Strand DNA Binding Proteins01:03

Single-Strand DNA Binding Proteins

For successful DNA replication, the unwinding of double-stranded DNA must be accompanied by stabilization and protection of the separated single strands of the DNA. This crucial task is performed by single-strand DNA-binding (SSB) proteins. They bind to the DNA in a sequence-independent manner, which means that the nitrogenous bases of the DNA need not be present in a specific order for binding of SSB proteins to it. The binding of SSB proteins straightens single-stranded DNA (ssDNA) and makes...
Homologous Recombination02:31

Homologous Recombination

The basic reaction of homologous recombination (HR) involves two chromatids that contain DNA sequences sharing a significant stretch of identity. One of these sequences uses a strand from another as a template to synthesize DNA in an enzyme-catalyzed reaction. The final product is a novel amalgamation of the two substrates. To ensure an accurate recombination of sequences, HR is restricted to the S and G2 phases of the cell cycle. At these stages, the DNA has been replicated already and the...
Restarting Stalled Replication Forks02:37

Restarting Stalled Replication Forks

DNA replication is initiated at sites containing predefined DNA sequences known as origins of replication. DNA is unwound at these sites by the minichromosome maintenance (MCM) helicase and other factors such as Cdc45 and the associated GINS complex.The unwound single strands are protected by replication protein A (RPA) until DNA polymerase starts synthesizing DNA at the 5’ end of the strand in the same direction as the replication fork. To prevent the replication fork from falling apart, a...
The DNA Replication Fork01:02

The DNA Replication Fork

An organism’s genome needs to be duplicated in an efficient and error-free manner for its growth and survival. The replication fork is a Y-shaped active region where two strands of DNA are separated and replicated continuously. The coupling of DNA unzipping and complementary strand synthesis is a characteristic feature of a replication fork.   Organisms with small circular DNA, such as E. coli, often have a single origin of replication; therefore, they have only two replication forks, one in...
Fixing Double-strand Breaks02:04

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The double-stranded structure of DNA has two major advantages. First, it serves as a safe repository of genetic information where one strand serves as the back-up in case the other strand is damaged. Second, the double-helical structure can be wrapped around proteins called histones to form nucleosomes, which can then be tightly wound to form chromosomes. This way, DNA chains up to 2 inches long can be contained within microscopic structures in a cell. A double-stranded break not only damages...

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Structural basis for the function of DEAH helicases.

Yangzi He1, Gregers R Andersen, Klaus H Nielsen

  • 1Department of Molecular Biology, Aarhus University, Aarhus, Denmark.

EMBO Reports
|February 20, 2010
PubMed
Summary
This summary is machine-generated.

The structure of yeast Prp43p reveals DEAH helicases are similar to DNA helicases. ATP binding likely alters a beta-hairpin, important for RNA unwinding and remodeling in splicing and ribosome biogenesis.

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • DEAH helicases are crucial enzymes involved in essential cellular processes such as pre-messenger RNA splicing and ribosome biogenesis.
  • Understanding the structural basis of DEAH helicase function is key to elucidating their roles in gene expression and cellular health.

Purpose of the Study:

  • To determine the three-dimensional structure of a yeast DEAH helicase, Prp43p, in complex with ADP.
  • To elucidate the structural features that dictate the enzymatic activity and substrate interactions of DEAH helicases.

Main Methods:

  • X-ray crystallography was employed to determine the high-resolution structure of yeast Prp43p-ADP.
  • Structural comparisons were made with known DNA helicases to identify conserved motifs and domains.

Main Results:

  • The structure revealed homology between DEAH helicases and DNA helicases, including an oligonucleotide-binding motif.
  • A key finding is a beta-hairpin that obstructs the RNA-binding site, suggesting a regulatory mechanism.
  • ATP binding and hydrolysis are hypothesized to induce conformational changes in the beta-hairpin, facilitating RNA unwinding or RNP remodeling.

Conclusions:

  • The determined structure of Prp43p provides a structural blueprint for understanding the mechanism of DEAH helicases.
  • This framework will facilitate future functional and genetic studies of the entire DEAH helicase family.