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Protein Complexes with Interchangeable Parts

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...

Protein Complexes with Interchangeable Parts

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...

Protein Complex Assembly

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...

Protein Complex Assembly

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...

Yeast Signaling

Yeast Signaling

Yeasts are single-celled organisms, but unlike bacteria, they are eukaryotes (cells with a nucleus). Cell signaling in yeast is similar to signaling in other eukaryotic cells. A ligand, such as a protein or a small molecule released from a yeast cell, attaches to a receptor on the cell surface. The binding stimulates second-messenger kinases to activate or inactivate transcription factors that further regulate gene expression. Many of the yeast intracellular signaling cascades have similar...

Covalently Linked Protein Regulators

Covalently Linked Protein Regulators

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.
These groups modify specific amino acids in a protein.

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Related Experiment Video

Updated: Jul 14, 2026

Identification of protein complexes with quantitative proteomics in S. cerevisiae

Identification of protein complexes with quantitative proteomics in S. cerevisiae

Published on: March 4, 2009

Protein coevolution and isoexpression in yeast macromolecular complexes.

Laurence Ettwiller¹, Reiner A Veitia

¹CNRS UMR 7637, Ecole Supérieure de Physique et de Chimie Industrielles, 10 rue Vauquelin, 75005 Paris, France.

Comparative and Functional Genomics

|June 1, 2007

Summary

Proteins within yeast macromolecular complexes exhibit coordinated evolutionary rates and expression levels. This coordination is more pronounced in real complexes than in randomized gene groups, suggesting functional implications.

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Last Updated: Jul 14, 2026

Identification of protein complexes with quantitative proteomics in S. cerevisiae

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Published on: March 4, 2009

Utilization of Grafix for the Detection of Transient Interactors of Saccharomyces cerevisiae Spliceosome Subcomplexes

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The Multifaceted Benefits of Protein Co-expression in Escherichia coli

The Multifaceted Benefits of Protein Co-expression in Escherichia coli

Published on: February 5, 2015

Area of Science:

Molecular Biology
Evolutionary Biology
Systems Biology

Background:

Genes encoding subunits of macromolecular complexes in Saccharomyces cerevisiae show similar evolutionary rates (K) and expression levels (E).
Gene expression levels (E) are known predictors of evolutionary rates (K), indicating a correlation between E and K.

Purpose of the Study:

To investigate the relationship between intracomplex variation of subunit expression and evolutionary rates.
To determine if proteins within real complexes exhibit coordinated expression and evolutionary rates compared to randomized groups.

Main Methods:

Analysis of intracomplex variation in gene expression (E) and evolutionary rates (K) using two dispersion measures.
Development of a mathematical transformation to create compound variables for intracomplex variation of E and K.
Comparison of compound variable values between real protein complexes and randomized gene sets.

Main Results:

Intracomplex variation in subunit expression correlates with intracomplex variation in evolutionary rates.
This correlation was also observed in randomized complexes, suggesting a need for further analysis.
Compound variables capturing simultaneous intracomplex variation of E and K were significantly smaller for real complexes than for randomized ones.

Conclusions:

Proteins within real macromolecular complexes demonstrate a tendency for more synchronized expression levels and evolutionary rates compared to randomly grouped genes.
This finding suggests potential functional or structural constraints driving the co-evolution of gene expression and protein evolution within complexes.
Further research is needed to explore the specific implications of this coordinated regulation.