2018
DOI: 10.1016/j.ijbiomac.2017.11.101
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New paradigm in ankyrin repeats: Beyond protein-protein interaction module

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Cited by 35 publications
(31 citation statements)
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“…However, most commonly, the permissivity of known eukaryotic hosts to giant viruses differs considerably according to the host strain or to the viral family or lineage, as previously described for mimiviruses, pandoraviruses, and Bodo saltans virus 32,48 . The analysis of giant virus homologs in the V. vermiformis genome showed here that the most represented sequences were those of giant viruses that grew in V. vermiformis, including faustovirus isolates and Orpheovirus IHUMI-LCC2, whereas a small proportion included genes from giant viruses isolated from Acanthamoeba spp.. Ankyrin repeats, which are associated with protein-protein interactions, were highly represented among V. vermiformis genes best matching with giant viruses 49,50 in addition to DUF4114 domains which are conserved domains that help to adapt to nutrient-depleted conditions by down-regulating protein biosynthesis 51 . Overall, the phylogenies of genes predicted to have arisen www.nature.com/scientificreports www.nature.com/scientificreports/ through lateral sequence transfer illustrate the complexity of sequence exchanges between amoebae, bacteria (including CPR), and giant viruses.…”
Section: Discussionmentioning
confidence: 83%
“…However, most commonly, the permissivity of known eukaryotic hosts to giant viruses differs considerably according to the host strain or to the viral family or lineage, as previously described for mimiviruses, pandoraviruses, and Bodo saltans virus 32,48 . The analysis of giant virus homologs in the V. vermiformis genome showed here that the most represented sequences were those of giant viruses that grew in V. vermiformis, including faustovirus isolates and Orpheovirus IHUMI-LCC2, whereas a small proportion included genes from giant viruses isolated from Acanthamoeba spp.. Ankyrin repeats, which are associated with protein-protein interactions, were highly represented among V. vermiformis genes best matching with giant viruses 49,50 in addition to DUF4114 domains which are conserved domains that help to adapt to nutrient-depleted conditions by down-regulating protein biosynthesis 51 . Overall, the phylogenies of genes predicted to have arisen www.nature.com/scientificreports www.nature.com/scientificreports/ through lateral sequence transfer illustrate the complexity of sequence exchanges between amoebae, bacteria (including CPR), and giant viruses.…”
Section: Discussionmentioning
confidence: 83%
“…At a molecular level, all TRPCs consist of a poreloop motif, three to four NH 2 -terminal ankyrin repeat domains (ARDs), and a COOH-terminal TRP domain (Venkatachalam and Montell, 2007). The ARD is a common protein-protein interaction module, typically consisting of 33 amino acid residues, which forms a canonical helix-loop-helix fold followed by a β-hairpin loop (Islam et al, 2018). ARDs perform crucial roles in various cellular processes, including thetranscription, signal transduction, inflammatory responses, cell development, and cell cycle (Islam et al, 2018).…”
Section: The Trpc Subfamily and Their Roles In Cnsmentioning
confidence: 99%
“…One of these scaffold proteins comprises repeated proteins that are naturally used for a wide variety of protein–protein interactions. In other words, these repeat proteins act as “antibodies” in nature . The designed anykrin repeat proteins (DARPins) are composed of completely recited repeats, which usually contain 33 amino acid residues.…”
Section: Introductionmentioning
confidence: 99%
“…In other words, these repeat proteins act as "antibodies" in nature. 15,16 The designed anykrin repeat proteins (DARPins) are composed of completely recited repeats, which usually contain 33 amino acid residues. Each repeat has a single structure, which includes a beta-turn and the subsequent two antiparallel alpha helixes, and over 29 consecutive repeats that can be observed in a single protein.…”
Section: Introductionmentioning
confidence: 99%