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Related Concept Videos

Protein Organization01:13

Protein Organization

Overview
Protein Folding01:22

Protein Folding

Overview
Protein Organization01:13

Protein Organization

Overview
Protein Organization01:24

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.
Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Organization01:24

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.

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Secondary Structural Model of Human MALAT1 Reveals Multiple Structure-Function Relationships.

Phillip J McCown1, Matthew C Wang1, Luc Jaeger2

  • 1Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN 46556, USA.

International Journal of Molecular Sciences
|November 14, 2019
PubMed
Summary
This summary is machine-generated.

Researchers modeled the structure of the long noncoding RNA MALAT1, revealing conserved elements and dynamic regions. This structural understanding offers new insights into MALAT1

Keywords:
MALAT1cancerlong noncoding RNAm6Asecondary structure

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Area of Science:

  • Molecular Biology
  • Genomics
  • RNA Biology

Background:

  • The long noncoding RNA MALAT1 is abundant in the nucleus and plays significant roles in various cancers.
  • While MALAT1's interacting partners and sequence conservation are known, its structural characteristics remain largely uncharacterized.

Purpose of the Study:

  • To propose a hypothetical secondary structural model for human MALAT1.
  • To identify evolutionarily conserved structural elements within MALAT1.
  • To explore potential structure-function relationships, including the impact of mutations and modifications on MALAT1 structure and microRNA binding.

Main Methods:

  • Development of a hypothetical secondary structural model for 8425 nucleotides of human MALAT1.
  • Integration of three experimental datasets probing RNA structure in vitro and in human cell lines.
  • Application of evolutionary conservation and covariation analyses using mammalian and vertebrate MALAT1 homologs.
  • Data mining to investigate the effects of RNA modifications, somatic mutations, and SNPs on MALAT1 structure.

Main Results:

  • The model predicts that approximately half of human MALAT1 is structured, featuring 194 helices, 13 pseudoknots, and numerous other structural motifs.
  • Evolutionary analyses support the conservation of 153 helices in mammalian and 42 in vertebrate MALAT1 homologs, highlighting a conserved core.
  • RNA modifications, cancer-associated mutations, and SNPs may induce structural changes affecting microRNA binding sites.

Conclusions:

  • The study provides a novel structural model for human MALAT1, revealing significant secondary structure and conserved elements.
  • The identified structure-function relationships offer mechanistic insights into MALAT1's roles in cancer.
  • The dynamic nature of MALAT1 structure is proposed to underlie its biological functions, particularly in cancer pathogenesis.