Evolution of EF-hand calcium-modulated proteins. II. Domains of several subfamilies have diverse evolutionary histories

@article{Nakayama2004EvolutionOE,
  title={Evolution of EF-hand calcium-modulated proteins. II. Domains of several subfamilies have diverse evolutionary histories},
  author={Susumu Nakayama and Nancy D Moncrief and Robert H. Kretsinger},
  journal={Journal of Molecular Evolution},
  year={2004},
  volume={34},
  pages={416-448}
}
SummaryIn the first report in this series we described the relationships and evolution of 152 individual proteins of the EF-hand subfamilies. Here we add 66 additional proteins and define eight (CDC, TPNV, CLNB, LPS, DGK, 1 F8, VIS, TCBP) new subfamilies and seven (CAL, SQUD, CDPK, EFH5, TPP, LAV, CRGP) new unique proteins, which we assume represent new subfamilies.The main focus of this study is the classification of individual EF-hand domains. Five subfamilies—calmodulin, troponin C… 
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95 Citations
Background Citations
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Methods Citations
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95 Citations

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Evolution of EF-hand calcium-modulated proteins. IV. Exon shuffling did not determine the domain compositions of EF-hand Proteins
TLDR
In the EF-hand family exons do not correspond to structural domains and exon shuffling played little if any role in the evolution of this widely distributed homolog family.
Evolution of EF-hand calcium-modulated proteins. III. Exon sequences confirm most dendrograms based on protein sequences: Calmodulin dendrograms show significant lack of parallelism
TLDR
It is concluded that exon shuffling did not play a significant role in the evolution of the EF-hand family and significant differences between protein and DNA trees for calmodulin remain unexplained.
Diversification and Independent Evolution of Troponin C Genes in Insects
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The results suggest that the rapid increase in number and sequence specialization of the adult Type III isoforms can be correlated with the evolution of the holometabolous mode of development and the acquisition of asynchronous indirect flight muscle function in insects.
Evolution of EF-hand calcium-modulated proteins. V. The genes encoding EF-hand proteins are not clustered in mammalian genomes
TLDR
No linkage has been found for genes encoding EF-hand proteins, indicating absence of selective pressure for maintaining chromosomal clustering, and suggests that chromosomal translocations occurred before divergence of these species.
Molecular cloning and evolutionary analysis of the calcium-modulated contractile protein, centrin, in green algae and land plants
TLDR
Phylogenetic relationships inferred from centrin-coding region comparisons mirror results of small subunit ribosomal RNA sequence analyses suggesting that centrin -coding regions are useful evolutionary markers within the green algae.
Dissecting the domain structure of Cdc4p, a myosin essential light chain involved in Schizosaccharomyces pombe cytokinesis.
TLDR
NMR spectroscopy is used to compare the structure, stability, and dynamics of the isolated N- and C-terminal domains of Cdc4p to hypothesize that these properties reflect a conformational plasticity of the C-domain, which may allow Cdc3p to interact with several regulatory or contractile ring proteins necessary for cytokinesis.
Structural and functional diversity of EF‐hand proteins: Evolutionary perspectives
We have classified 865 sequences of EF‐hand proteins from five proteomes into 156 subfamilies. These subfamilies were put into six groups. Evolutionary relationships among subfamilies and groups were…
Insights into functional aspects of centrins from the structure of N-terminally extended mouse centrin 1
Domain Analysis of a Groundnut Calcium-dependent Protein Kinase
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CD spectroscopic analysis indicates the intramolecular structural changes accompanied with calcium binding to be similar to canonical CDPKs and the possible significance of obligatory coupling between the presence of NLS in the junction domain and atypical calcium binding properties of these C DPKs is discussed.
The Dictyostelium class I myosin, MyoD, contains a novel light chain that lacks high-affinity calcium-binding sites.
TLDR
Through its specific association with the Ca2+-insensitive MlcD, MyoD may exhibit distinct regulatory properties that distinguish it from myosin I isoenzymes with calmodulin light chains.
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