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Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Bacterial RNA Polymerase00:43

Bacterial RNA Polymerase

Unlike eukaryotes, bacteria use a single RNA Polymerase (RNAP) to transcribe all genes. The different subunits of bacterial RNAPhave distinct functions. The multisubunit structure of the bacterial RNAP helps the enzyme to maintain catalytic function, facilitate assembly, interact with DNA and RNA, and self-regulate its activity.
In most genes, the transcription site is a single base present upstream of the coding sequence. Though RNAP is a catalytically efficient enzyme, it does not recognize...
Bacterial Transcription01:53

Bacterial Transcription

RNA polymerase (RNAP) carries out DNA-dependent RNA synthesis in both bacteria and eukaryotes. Bacteria do not have a membrane-bound nucleus. So, transcription and translation occur simultaneously, on the same DNA template.
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Signal Sequences and Sorting Receptors01:41

Signal Sequences and Sorting Receptors

Signal sequences are short amino acid sequences that guide newly synthesized proteins to their proper location within the cell. Classical signal sequences are fifteen to sixty amino acids long and present at the N-terminus of a polypeptide chain. Each signal sequence has a conserved segment of basic residues towards their N terminus, a hydrophobic core, and a C-terminus rich in polar residues. The C-terminus also contains a signal cleavage site and features a -3 -1 sequence motif. The -3-1...
Exon Recombination02:32

Exon Recombination

The evolution of new genes is critical for speciation. Exon recombination, also known as exon shuffling or domain shuffling, is an important means of new gene formation. It is observed across vertebrates, invertebrates, and in some plants such as potatoes and sunflowers. During exon recombination, exons from the same or different genes recombine and produce new exon-intron combinations, which might evolve into new genes. 
Exon shuffling follows “splice frame rules.” Each exon has three reading...
Gene Duplication and Divergence02:37

Gene Duplication and Divergence

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 characterized.

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Related Experiment Video

Updated: Jun 10, 2026

Measuring RAN Peptide Toxicity in C. elegans
10:49

Measuring RAN Peptide Toxicity in C. elegans

Published on: April 30, 2020

Nebulin: a study of protein repeat evolution.

Asa K Björklund1, Sara Light, Rauan Sagit

  • 1Center for Biological Membrane Research, Stockholm Bioinformatics Center, Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.

Journal of Molecular Biology
|July 21, 2010
PubMed
Summary

Protein domain repeats, like those in the muscle protein Nebulin, expand via tandem duplications. These duplications, often involving super repeats (SRs), occur independently and are frequent in genes with repetitive domains.

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Area of Science:

  • Molecular Biology
  • Evolutionary Biology
  • Genomics

Background:

  • Protein domain repeats are crucial for cellular organization, particularly in eukaryotes.
  • Internal tandem duplications are a known mechanism for repeat evolution, but underlying processes remain unclear.
  • Nebulin, a muscle protein, features numerous actin-binding nebulin domains and serves as a model for studying repeat expansion.

Purpose of the Study:

  • To elucidate the mechanisms driving protein repeat expansion.
  • To investigate the evolutionary history of Nebulin and its domain repeats.
  • To determine the role of tandem duplications and super repeats in Nebulin evolution.

Main Methods:

  • Comparative genomic analysis of Nebulin evolution across species.
  • Identification and characterization of tandem duplication events in the Nebulin gene.
  • Analysis of duplication junctions and associated genomic elements (e.g., Alu transposons).
  • Examination of segmental duplication patterns in the human genome.

Main Results:

  • Nebulin evolved from a two-domain invertebrate precursor, with repeat regions expanding through single-domain and super repeat (SR) duplications.
  • SRs, comprising seven nebulin domains, evolved independently at least three times in invertebrates and vertebrates.
  • Recent tandem duplications in Nebulin involve single domains, SR units, or multiple SRs, often duplicating the same unit multiple times.
  • Duplication junctions frequently coincide with Alu transposons, suggesting Alu-mediated homologous recombination.
  • Duplications in SR regions consistently involve multiples of seven domains, but the duplicated unit varies.
  • Genes with domain repeats, especially long repeated genes, exhibit significantly higher rates of segmental duplication in the human genome.

Conclusions:

  • The large Nebulin protein arose not from simple tandem duplications of the same motif, but through complex, independent expansions involving single domains and multi-domain SRs.
  • Alu-mediated recombination appears to be a significant mechanism for tandem duplication in the Nebulin gene.
  • Genes containing domain repeats are predisposed to larger-scale duplications, indicating a general principle in genome evolution.