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Related Concept Videos

Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
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Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
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Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
RNA Polymerase II Accessory Proteins02:36

RNA Polymerase II Accessory Proteins

Proteins that regulate transcription can do so either via direct contact with RNA Polymerase or through indirect interactions facilitated by adaptors, mediators, histone-modifying proteins, and nucleosome remodelers. Direct interactions to activate transcription is seen in bacteria as well as in some eukaryotic genes. In these cases, upstream activation sequences are adjacent to the promoters, and the activator proteins interact directly with the transcriptional machinery. For example, in...
RNA Polymerase II Accessory Proteins02:36

RNA Polymerase II Accessory Proteins

Proteins that regulate transcription can do so either via direct contact with RNA Polymerase or through indirect interactions facilitated by adaptors, mediators, histone-modifying proteins, and nucleosome remodelers. Direct interactions to activate transcription is seen in bacteria as well as in some eukaryotic genes. In these cases, upstream activation sequences are adjacent to the promoters, and the activator proteins interact directly with the transcriptional machinery. For example, in...
The ADP/ATP Carrier Protein01:42

The ADP/ATP Carrier Protein

ADP/ATP carrier or AAC protein is the most abundant carrier protein in the inner mitochondrial membrane. It transports large quantities of ADP and ATP, equivalent to the average human body weight, every day. Among other transporters, ACC protein is one of the best-studied members of the mitochondrial carrier protein family. The ADP/ATP carrier protein comprises two transmembrane helices connected to a loop and a single alpha-helix on the matrix side. It switches between two conformational...

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High-resolution Melting PCR for Complement Receptor 1 Length Polymorphism Genotyping: An Innovative Tool for Alzheimer's Disease Gene Susceptibility Assessment
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APOBEC-1 complementation factor (ACF) forms RNA-dependent multimers.

C A Galloway1, A Kumar, J Krucinska

  • 1University of Rochester, School of Medicine and Dentistry, Department of Biochemistry and Biophysics, 601 Elmwood Ave., Rochester, NY 14642, USA.

Biochemical and Biophysical Research Communications
|June 15, 2010
PubMed
Summary
This summary is machine-generated.

Researchers created a truncated APOBEC-1 complementation factor (ACF320) that supports apoB mRNA editing. This ACF320 protein forms RNA-bridged homomultimers, suggesting a model for the editosome assembly.

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Artificial RNA Polymerase II Elongation Complexes for Dissecting Co-transcriptional RNA Processing Events

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Area of Science:

  • Molecular Biology
  • RNA Biology
  • Protein Engineering

Background:

  • APOBEC-1 complementation factor (ACF) is crucial for RNA editing.
  • Understanding ACF's structure and function is key to RNA editing mechanisms.
  • Previous studies lacked detailed structural insights into functional ACF domains.

Purpose of the Study:

  • To engineer a stable, functional, truncated ACF protein (ACF320).
  • To investigate the RNA binding and editing activity of ACF320.
  • To elucidate the in situ assembly and multimerization of ACF in the context of RNA editing.

Main Methods:

  • Limited proteolysis and computational secondary structure modeling to design ACF320.
  • RNA binding assays using apoB mRNA.
  • APOBEC-1 dependent editing activity assays.
  • Live cell Förster Resonance Energy Transfer (FRET) and immunoprecipitation assays.

Main Results:

  • ACF320, spanning residues 1-320 with three RNA recognition motifs (RRMs), was successfully constructed.
  • ACF320 demonstrated preferential binding to apoB mRNA.
  • ACF320 supported APOBEC-1 dependent editing at 40% of full-length ACF activity.
  • Live cell assays showed ACF320 forms RNA-bridged homomultimers in situ.

Conclusions:

  • The engineered ACF320 protein retains significant RNA binding and editing support functions.
  • ACF320's homomultimerization, bridged by RNA, provides insights into editosome assembly.
  • A model is proposed where the C to U editosome assembles as ACF-APOBEC-1 dimers on apoB mRNA.