Hundreds of ankyrin‐like repeats in functionally diverse proteins: Mobile modules that cross phyla horizontally?

@article{Bork1993HundredsOA,
  title={Hundreds of ankyrin‐like repeats in functionally diverse proteins: Mobile modules that cross phyla horizontally?},
  author={Peer Bork},
  journal={Proteins: Structure},
  year={1993},
  volume={17}
}
  • P. Bork
  • Published 1 December 1993
  • Biology
  • Proteins: Structure
Based on pattern searches and systematic database screening, almost 650 different ankyrin‐like (ANK) repeats from nearly all phyla have been identified; more than 150 of them are reported here for the first time. Their presence in functionally diverse proteins such as enzymes, toxins, and transcription factors strongly suggests domain shuffling, but their occurrence in prokaryotes and yeast excludes exon shuffling. The spreading mechanism remains unknown, but in at least three cases horizontal… 
Ankyrin domains across the Tree of Life
TLDR
Results support the hypothesis that intracellular bacteria broadly employ ANK repeats for structure-function relationships with the eukaryotic host cell and assess their widespread abundance in Bacteria and Archaea for the first time.
Sequence and Structure-Based Analyses of Human Ankyrin Repeats
Ankyrin is one of the most abundant protein repeat families found across all forms of life. It is found in a variety of multi-domain and single domain proteins in humans with diverse number of
The Diversity and Evolution of Wolbachia Ankyrin Repeat Domain Genes
TLDR
The results confirm previous findings that the Wolbachia genomes are evolutionary mosaics and illustrate the potential that these bacteria have to generate diversity in proteins potentially involved in the symbiotic interactions.
The ankyrin repeat as molecular architecture for protein recognition
TLDR
Characterization of the folding and assembly pathways suggests that ankyrin repeat domains generally undergo a two‐state folding transition despite their modular structure.
Designed to be stable: Crystal structure of a consensus ankyrin repeat protein
TLDR
The AR domain fold is an intrinsically very stable and well-expressed scaffold, able to display randomized interacting residues, and represents an excellent basis for the design of novel binding molecules.
Expansion and Function of Repeat Domain Proteins During Stress and Development in Plants
TLDR
The structure and functions of these repeat proteins have been extensively studied in plants suggesting a critical role of these repeating peptides in plant cell physiology, stress and development.
Global Analysis of Ankyrin Repeat Domain C3HC4-Type RING Finger Gene Family in Plants
TLDR
The preferential expression of XB3-like genes in specified tissues and the response to phytohormone and abiotic stress treatments of Arabidopsis and Zea mays not only confirmed the microarray analysis data but also demonstrated that the XB 3-like proteins play roles in plant growth and development as well as in stress responses.
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 47 REFERENCES
Analysis of cDNA for human erythrocyte ankyrin indicates a repeated structure with homology to tissue-differentiation and cell-cycle control proteins
Analysis of complementary DNA for human erythroid ankyrin indicates that the mature protein contains 1,880 amino acids comprising an N-terminal domain binding integral membrane proteins and tubulin,
Comprehensive sequence analysis of the 182 predicted open reading frames of yeast chromosome III
TLDR
It is suggested that the development of an automated computer workbench for protein sequence analysis must be an important item in genome projects because the information gap between known protein sequences and unknown function is expected to widen and become a major bottleneck of genome projects in the near future.
Proposed acquisition of an animal protein domain by bacteria.
  • P. Bork, R. Doolittle
  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 1992
A systematic screen of a protein sequence data base confirms that the fibronectin type III (Fn3) domain is widely distributed among animal proteins and occurs also in several bacterial
Ancient conserved regions in new gene sequences and the protein databases.
TLDR
Nearly all of the ACRs identified were found to be homologous to sequences in the protein databases, suggesting that currently known proteins may already include representatives of most ACRs and that new sequences not similar to any database sequence are unlikely to contain ACRs.
Convergence of Ets- and notch-related structural motifs in a heteromeric DNA binding complex.
TLDR
Observations provide evidence for a distinct biochemical role for the 33-amino acid repeats of GABP beta, and suggest that they may serve as a module for the generation of specific dimerization interfaces.
Dense Alu clustering and a potential new member of the NFκB family within a 90 kilobase HLA Class III segment
TLDR
A detailed structural analysis of 90 kilobases of the HLA Class III region from the Bat2 gene at the centromeric end to 23 kb beyond TNF is conducted, finding that this region contains four known genes and a novel telomeric potential coding region.
Reconstructing history with amino acid sequences 1
The main goal of the protein evolutionist is the reconstruction of past events leading to the structures of contemporary proteins. The common strategy is to align amino acid sequences and make
...
1
2
3
4
5
...