PUBLICATION

Molecular cloning and functional characterization of zebrafish ATM

Authors
Imamura, S., and Kishi, S.
ID
ZDB-PUB-050308-3
Date
2005
Source
The international journal of biochemistry & cell biology   37(5): 1105-1116 (Journal)
Registered Authors
Kishi, Shuji
Keywords
A-T; ATM; Zebrafish; DNA damage; Aging
MeSH Terms
  • Aging
  • Amino Acid Sequence
  • Animals
  • Ataxia Telangiectasia/genetics
  • Ataxia Telangiectasia Mutated Proteins
  • Base Sequence
  • Cell Cycle Proteins/chemistry
  • Cell Cycle Proteins/genetics*
  • Cell Cycle Proteins/physiology*
  • Cloning, Molecular
  • DNA Damage
  • DNA-Binding Proteins/chemistry
  • DNA-Binding Proteins/genetics*
  • DNA-Binding Proteins/physiology*
  • Disease Models, Animal
  • Humans
  • Mice
  • Molecular Sequence Data
  • Protein Serine-Threonine Kinases/chemistry
  • Protein Serine-Threonine Kinases/genetics*
  • Protein Serine-Threonine Kinases/physiology*
  • Tumor Suppressor Proteins/chemistry
  • Tumor Suppressor Proteins/genetics*
  • Tumor Suppressor Proteins/physiology*
  • Zebrafish/genetics
  • Zebrafish Proteins/chemistry
  • Zebrafish Proteins/genetics*
  • Zebrafish Proteins/physiology*
PubMed
15743681 Full text @ Int. J. Biochem. Cell Biol.
Abstract
Ataxia-telangiectasia mutated (ATM) is the gene product mutated in ataxia-telangiectasia (A-T), which is an autosomal recessive disorder with symptoms including neurodegeneration, cancer predisposition and premature aging. ATM is thought to play a pivotal role in signal transduction in response to genotoxic DNA damage. To study the physiological and developmental functions of ATM using the zebrafish model system, we cloned the zebrafish homolog cDNA of human ATM (hATM), zebrafish ATM (zATM), analyzed the expression pattern of zATM during early development, and further developed the system to study loss of zATM function in zebrafish embryos. Employing information available from the zebrafish genomic database, we utilized a PCR-based approach to isolate zATM cDNA clones. Sequence analysis of zATM showed a high level homology in the functional domains of hATM. The putative FAT, phosphoinositide 3-kinase-like, and FATC domains of zATM, which regulate ATM kinase activity and functions, were the most highly conserved regions, exhibiting 64-94% amino acid identity to the corresponding domains in hATM, while exhibiting approximately 50% amino acid identity outside these domains. The zATM gene is expected to consist of 62 coding exons, and we have identified at least 55 exons encompassing more than 100kb of nucleotide sequence, which encodes about 9kb of cDNA. By in situ hybridization, zATM mRNA was detected ubiquitously with a dramatic increase at the 18-somite stage, then more specifically in the eye, brain, trunk, and tail at later stages. To inhibit zATM expression and function, we designed and synthesized splice-blocking antisense-morpholino oligonucleotides targeting the phosphoinositide 3-kinase-like domain. We demonstrated that this knockdown of zATM caused abnormal development upon ionizing radiation-induced DNA damage. Our data suggest that the ATM gene is structurally and functionally conserved in vertebrates from zebrafish to human.
Genes / Markers
Figures
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Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Antibodies
Orthology
Engineered Foreign Genes
Mapping