Related Experiment Video
Updated: May 19, 2026

10:11
Hybrid Ensemble and Single-molecule Assay to Image the Motion of Fully Reconstituted CMG
Published on: July 26, 2024
The origin recognition complex: a biochemical and structural view.
1Department of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, NY, 11794, USA, hli@bnl.gov.
Sub-Cellular Biochemistry
|August 25, 2012
Summary
The origin recognition complex (ORC) is an ATP-dependent machine crucial for eukaryotic DNA replication. Recent structural studies reveal its role in forming pre-replicative complexes at DNA origins to initiate DNA duplication.
Area of Science:
- Molecular Biology
- Cell Biology
- Biochemistry
Background:
- The origin recognition complex (ORC) was discovered in yeast in 1992.
- ORC's identification enabled investigations into eukaryotic genome duplication control.
- Recent advances in electron microscopy are providing structural insights into ORC.
Purpose of the Study:
- To outline current biochemical knowledge of ORC across eukaryotic systems.
- To emphasize recent structural and biochemical studies on ORC.
- To highlight ORC's conserved function in initiating DNA replication.
Main Methods:
- Review of existing biochemical data on ORC.
- Analysis of recent electron microscopy and image reconstruction studies.
- Comparative analysis across different eukaryotic systems.
Main Results:
- ORC is an ATP-dependent machine.
- ORC recruits proteins to form pre-replicative complexes (pre-RCs).
- Pre-RC formation occurs at origins of DNA replication.
Conclusions:
- ORC plays a conserved role in initiating DNA replication in eukaryotic cells.
- Despite species-specific variations, ORC functions as a core component of the DNA replication machinery.
- Structural and biochemical data are converging to define ORC's mechanism of action.
Related Concept Videos
Assembly of Signaling Complexes
Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
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.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
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.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
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...
Many viruses self-assemble into a fully functional unit using the infected host cell to...
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...
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Chromosome Structure
A functional eukaryotic chromosome must contain three elements: a centromere, telomeres, and numerous origins of replication.
The centromere is a DNA sequence that links sister chromatids. This is also where kinetochores, protein complexes to which spindle microtubules attach, are constructed after the chromosome is replicated. The kinetochores allow the spindle microtubules to move the chromosomes within the cell during cell division.
Telomeres consist of non-coding repetitive nucleotide...
The centromere is a DNA sequence that links sister chromatids. This is also where kinetochores, protein complexes to which spindle microtubules attach, are constructed after the chromosome is replicated. The kinetochores allow the spindle microtubules to move the chromosomes within the cell during cell division.
Telomeres consist of non-coding repetitive nucleotide...

