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Related Concept Videos

Protein Families02:47

Protein Families

15.3K
Protein families are groups of homologous proteins; that is, they have similarities in amino acid sequences and three-dimensional structures. Protein families usually occur because of gene duplication, where an additional copy of a gene is inserted into the genome of an organism.   Mutations that change the amino acids but still allow the protein to be properly synthesized, will lead to new protein family members.   If these new proteins contain similar amino acids in key...
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Gene Families01:57

Gene Families

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Gene families consist of groups of genes proposed to have originated from a common ancestor. Typically these arise through events in which a gene or genes are mistakenly duplicated during cell division. Unlike their parent genes (which are subject to selection pressure to maintain function), these gene copies do not need to preserve their sequences and may evolve at a relatively faster rate.
Occasionally these regions can be adapted to take on new roles within the organism, becoming novel genes...
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Gene Duplication and Divergence02:37

Gene Duplication and Divergence

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The seminal work of Ohno in 1970 popularized the idea of gene duplication and divergence. DNA sequence comparison studies reveal that a large portion of the genes in bacteria, archaebacteria, and eukaryotes was  generated by gene duplication and divergence, indicating its critical role in evolution.
The duplicated copies of the gene are called Paralogs. Paralogs with similar sequences and functions form a gene family. Across several species, a large number of gene families are...
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Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

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In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as...
5.2K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

2.5K
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...
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Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

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Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
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Updated: Jun 12, 2025

Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous &#946;2-Microglobulin
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Stability and Structure of Bat Major Histocompatibility Complex Class I with Heterologous β2-Microglobulin

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Functional diversification within the heme-binding split-barrel family.

Nicolas Grosjean1, Lifang Zhang2, Desigan Kumaran1

  • 1Biology Department, Brookhaven National Laboratory, Upton, New York, USA.

The Journal of Biological Chemistry
|October 12, 2024
PubMed
Summary
This summary is machine-generated.

Researchers identified a large family of heme-binding proteins (homolog of HugZ) with diverse roles in heme metabolism across bacteria, plants, and algae. Disrupting these proteins in plants caused developmental issues, highlighting their biological importance.

Keywords:
AT1G51560AT3G03890AT3G21140GluTRBPHOZHOZ2AHOZ2Bchloroplastiron

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Measurement of Heme Synthesis Levels in Mammalian Cells
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Measurement of Heme Synthesis Levels in Mammalian Cells
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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Proteins with similar structures can evolve distinct functions through neofunctionalization after gene duplication.
  • Sequence similarity alone is insufficient for functional annotation of divergent homologous proteins.
  • Heme metabolism is crucial in various organisms, involving both enzymatic degradation and nonenzymatic sensing.

Purpose of the Study:

  • To identify and characterize a multifunctional protein family involved in heme metabolism.
  • To elucidate the evolutionary and functional diversity of the homolog of HugZ (HOZ) family.
  • To understand the sequence-structure-function relationships of heme-binding proteins across different lineages.

Main Methods:

  • Bioinformatic analysis to identify the HOZ family within the FMN-binding split barrel superfamily.
  • Targeted experimentation including in vitro heme degradation assays.
  • Genetic disruption experiments in Arabidopsis thaliana and structural characterization of Populus trichocarpa homologs.

Main Results:

  • A large, multifunctional HOZ protein family was identified across prokaryotes, plants, and algae, binding heme and participating in its metabolism.
  • Prokaryotic HOZ proteins are linked to iron assimilation; plant and algal HOZ proteins are involved in heme degradation or biosynthesis regulation.
  • Disruption of HOZ1 and HOZ2 in Arabidopsis thaliana led to developmental delays, indicating essential plastid roles. A cytosolic paralog in Populus trichocarpa retained conserved heme-binding sites.

Conclusions:

  • This study unifies the understanding of sequence-structure-function relationships within the multilineage HOZ family.
  • New molecular players in plant and bacterial heme metabolism have been identified.
  • The HOZ family represents a significant component of heme management across diverse life forms.