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Mutations

Mutations

Mutations

Mutations

Mutations are changes in the sequence of DNA. These changes can occur spontaneously or they can be induced by exposure to environmental factors. Mutations can be characterized in a number of different ways: whether and how they alter the amino acid sequence of the protein, whether they occur over a small or large area of DNA, and whether they occur in somatic cells or germline cells.
Chromosomal Alterations Are Large-Scale Mutations
While point mutations are changes in a single nucleotide in...

Assembly of Complex Microtubule Structures

Assembly of Complex Microtubule Structures

Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.

Viral Mutations

Viral Mutations

A mutation is a change in the sequence of bases of DNA or RNA in a genome. Some mutations occur during replication of the genome due to errors made by the polymerase enzymes that replicate DNA or RNA. Unlike DNA polymerase, RNA polymerase is prone to errors because it is not capable of “proofreading” its work. Viruses with RNA-based genomes, like HIV, therefore accrue mutations faster than viruses with DNA-based genomes. Because mutation and recombination provide the raw material...

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...

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...

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Structural Mapping of Missense Mutations in the Pex1/Pex6 Complex.

Anne Schieferdecker¹, Petra Wendler²

¹Institute of Biochemistry and Biology, University of Potsdam, D-14476 Potsdam, Germany.

International Journal of Molecular Sciences

|August 4, 2019

Summary

Peroxisome biogenesis disorders (PBDs) stem from mutations in Pex1/Pex6 proteins crucial for peroxisome function. Mapping mutations onto a homology model helps classify them, distinguishing between destabilizing and function-impairing types for potential therapeutic strategies.

Keywords:

Pex1 Pex6 Zellweger Zellweger syndrome spectrum disorder (ZSSD)mutation structure

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Area of Science:

Biochemistry
Genetics
Cell Biology

Background:

Peroxisome biogenesis disorders (PBDs) are severe inherited diseases lacking effective treatments.
Mutations in PEX1 and PEX6 genes account for ~65% of PBD cases, affecting the Pex1/Pex6 complex essential for peroxisomal protein import.
No high-resolution structural data exists for the human Pex1/Pex6 AAA+ ATPase complex.

Purpose of the Study:

To classify and rationalize missense mutations in PEX1 and PEX6 found in PBD patients.
To map these mutations onto a homology model of the human Pex1/Pex6 complex.
To differentiate mutation types and their potential implications for therapeutic interventions.

Main Methods:

Literature review of reported missense mutations in PBD patients.
Construction of a homology model for the human Pex1/Pex6 complex.
Mapping identified mutations onto the homology model to assess their functional and structural impact.

Main Results:

Several PBD-associated mutations were mapped to functionally conserved residues within the Pex1/Pex6 complex.
These mutations are implicated in critical processes like ATP hydrolysis and substrate handling.
A distinction was made between mutations that destabilize the protein fold and those that impair function.

Conclusions:

The homology model provides a framework for understanding PEX1/PEX6 mutation effects in PBDs.
Function-impairing mutations may not respond to stabilizing agents, unlike fold-destabilizing mutations.
This classification is crucial for developing targeted therapeutic strategies for PBD patients.