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Related Concept Videos

Multi-species Conserved Sequences02:51

Multi-species Conserved Sequences

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Next-generation sequencing technologies have created large genomic databases of a variety of animals and plants. Ever since the human genome project was completed, scientists studied the genome of primates, mammals, and other phylogenetically distant living beings. Such large-scale  studies have provided new insights into the evolutionary relationship between organisms.
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Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
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Cis-regulatory sequences are short fragments of non-coding DNA that are present on the same chromosomes as the genes that they regulate. These fragments serve as binding sites for transcriptional regulators, proteins that are responsible for controlling gene transcription and differential gene expression across cell types in eukaryotes. Cis-regulatory sequences can be close to the gene of interest or thousands of bases away in the DNA sequence; however, those sequences that are further away are...
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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.
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High Resolution Whole Mount In Situ Hybridization within Zebrafish Embryos to Study Gene Expression and Function
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Tilapia and human CLIC2 structures are highly conserved.

Jiao Zeng1, Zhengjun Li2, Eei Yin Lui2

  • 1Department of Biological Sciences, National University of Singapore 117543, Singapore.

Biochemical and Biophysical Research Communications
|December 5, 2017
PubMed
Summary
This summary is machine-generated.

The crystal structure of tilapia Chloride intracellular channel 2 (CLIC2) reveals high conservation among vertebrates. Its tissue-specific expression suggests a role in iono-osmoregulation during extreme environmental changes.

Keywords:
CLIC2CXXC motifCrystal structureGlutaredoxin foldGlutathione S-Transferase (GST) fold

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Physiology

Background:

  • Chloride intracellular channels (CLICs) are a family of proteins with both soluble and membrane-bound forms.
  • CLICs are implicated in various cellular functions, including ion transport and cell volume regulation.
  • Understanding the structure and function of CLICs is crucial for elucidating their roles in cellular physiology.

Purpose of the Study:

  • To determine the crystal structure of soluble Chloride intracellular channel 2 (CLIC2) from the euryhaline teleost fish Oreochromis mossambicus.
  • To compare the structural conservation of tilapia CLIC2 with human CLIC2 and other CLIC proteins.
  • To investigate the expression patterns of clic2 in tilapia osmoregulatory organs under different salinity conditions.

Main Methods:

  • X-ray crystallography was used to determine the three-dimensional structure of soluble tilapia CLIC2.
  • Bioinformatic tools were employed for structural comparisons between different CLIC proteins.
  • Quantitative analysis of clic2 gene expression was performed in tilapia tissues acclimated to varying salinities (freshwater, seawater, hypersaline water).

Main Results:

  • The crystal structure of soluble tilapia CLIC2 was successfully determined, revealing its molecular architecture.
  • Structural analysis indicated a high degree of conservation between tilapia CLIC2, human CLIC2, and other vertebrate CLICs.
  • Significant tissue-specific expression of clic2 was observed in tilapia, with notable responsiveness to different salinity levels.

Conclusions:

  • The high structural conservation of vertebrate CLIC2 suggests conserved functional roles across species.
  • The tissue-specific and salinity-dependent expression of clic2 in tilapia points towards its involvement in iono-osmoregulation, particularly under challenging environmental conditions.
  • Further research into CLIC proteins could uncover novel insights into ion transport mechanisms and osmoregulatory strategies in teleost fish.