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Jack A M Leunissen - One of the best experts on this subject based on the ideXlab platform.

  • genealogy of the α crystallin small heat shock protein superfamily
    International Journal of Biological Macromolecules, 1998
    Co-Authors: W.w. De Jong, Gertjan Caspers, Jack A M Leunissen
    Abstract:

    Sequences of 40 very diverse representatives of the alpha-crystallin-small heat-shock protein (alpha-Hsp) superfamily are compared. Their characteristic C-terminal 'alpha-crystallin domain' of 80-100 residues contains short consensus sequences that are highly conserved from prokaryotes to Eukaryotes. There are, in addition, some positions that clearly distinguish animal from non-animal alpha-Hsps. The alpha-crystallin domain is predicted to consist of two hydrophobic beta-sheet motifs, separated by a hydrophilic region which is variable in length. Combination of a conserved alpha-crystallin domain with a variable N-terminal domain and C-terminal extension probably modulates the properties of the various alpha-Hsps as stress-protective and structural oligomeric proteins. Phylogeny reconstruction indicates that multiple alpha-Hsps were already present in the last common ancestor of pro- and Eukaryotes. It is suggested that during Eukaryote Evolution, animal and non-animal alpha-Hsps originated from different ancestral gene copies. Repeated gene duplications gave rise to the multiple alpha-Hsps present in most organisms.

  • genealogy of the α crystallin small heat shock protein superfamily
    International Journal of Biological Macromolecules, 1998
    Co-Authors: W.w. De Jong, Gertjan Caspers, Jack A M Leunissen
    Abstract:

    Sequences of 40 very diverse representatives of the α-crystallin–small heat-shock protein (α-Hsp) superfamily are compared. Their characteristic C-terminal `α-crystallin domain' of 80–100 residues contains short consensus sequences that are highly conserved from prokaryotes to Eukaryotes. There are, in addition, some positions that clearly distinguish animal from non-animal α-Hsps. The α-crystallin domain is predicted to consist of two hydrophobic β-sheet motifs, separated by a hydrophilic region which is variable in length. Combination of a conserved α-crystallin domain with a variable N-terminal domain and C-terminal extension probably modulates the properties of the various α-Hsps as stress-protective and structural oligomeric proteins. Phylogeny reconstruction indicates that multiple α-Hsps were already present in the last common ancestor of pro- and Eukaryotes. It is suggested that during Eukaryote Evolution, animal and non-animal α-Hsps originated from different ancestral gene copies. Repeated gene duplications gave rise to the multiple α-Hsps present in most organisms.

W.w. De Jong - One of the best experts on this subject based on the ideXlab platform.

  • genealogy of the α crystallin small heat shock protein superfamily
    International Journal of Biological Macromolecules, 1998
    Co-Authors: W.w. De Jong, Gertjan Caspers, Jack A M Leunissen
    Abstract:

    Sequences of 40 very diverse representatives of the alpha-crystallin-small heat-shock protein (alpha-Hsp) superfamily are compared. Their characteristic C-terminal 'alpha-crystallin domain' of 80-100 residues contains short consensus sequences that are highly conserved from prokaryotes to Eukaryotes. There are, in addition, some positions that clearly distinguish animal from non-animal alpha-Hsps. The alpha-crystallin domain is predicted to consist of two hydrophobic beta-sheet motifs, separated by a hydrophilic region which is variable in length. Combination of a conserved alpha-crystallin domain with a variable N-terminal domain and C-terminal extension probably modulates the properties of the various alpha-Hsps as stress-protective and structural oligomeric proteins. Phylogeny reconstruction indicates that multiple alpha-Hsps were already present in the last common ancestor of pro- and Eukaryotes. It is suggested that during Eukaryote Evolution, animal and non-animal alpha-Hsps originated from different ancestral gene copies. Repeated gene duplications gave rise to the multiple alpha-Hsps present in most organisms.

  • genealogy of the α crystallin small heat shock protein superfamily
    International Journal of Biological Macromolecules, 1998
    Co-Authors: W.w. De Jong, Gertjan Caspers, Jack A M Leunissen
    Abstract:

    Sequences of 40 very diverse representatives of the α-crystallin–small heat-shock protein (α-Hsp) superfamily are compared. Their characteristic C-terminal `α-crystallin domain' of 80–100 residues contains short consensus sequences that are highly conserved from prokaryotes to Eukaryotes. There are, in addition, some positions that clearly distinguish animal from non-animal α-Hsps. The α-crystallin domain is predicted to consist of two hydrophobic β-sheet motifs, separated by a hydrophilic region which is variable in length. Combination of a conserved α-crystallin domain with a variable N-terminal domain and C-terminal extension probably modulates the properties of the various α-Hsps as stress-protective and structural oligomeric proteins. Phylogeny reconstruction indicates that multiple α-Hsps were already present in the last common ancestor of pro- and Eukaryotes. It is suggested that during Eukaryote Evolution, animal and non-animal α-Hsps originated from different ancestral gene copies. Repeated gene duplications gave rise to the multiple α-Hsps present in most organisms.

Gertjan Caspers - One of the best experts on this subject based on the ideXlab platform.

  • genealogy of the α crystallin small heat shock protein superfamily
    International Journal of Biological Macromolecules, 1998
    Co-Authors: W.w. De Jong, Gertjan Caspers, Jack A M Leunissen
    Abstract:

    Sequences of 40 very diverse representatives of the alpha-crystallin-small heat-shock protein (alpha-Hsp) superfamily are compared. Their characteristic C-terminal 'alpha-crystallin domain' of 80-100 residues contains short consensus sequences that are highly conserved from prokaryotes to Eukaryotes. There are, in addition, some positions that clearly distinguish animal from non-animal alpha-Hsps. The alpha-crystallin domain is predicted to consist of two hydrophobic beta-sheet motifs, separated by a hydrophilic region which is variable in length. Combination of a conserved alpha-crystallin domain with a variable N-terminal domain and C-terminal extension probably modulates the properties of the various alpha-Hsps as stress-protective and structural oligomeric proteins. Phylogeny reconstruction indicates that multiple alpha-Hsps were already present in the last common ancestor of pro- and Eukaryotes. It is suggested that during Eukaryote Evolution, animal and non-animal alpha-Hsps originated from different ancestral gene copies. Repeated gene duplications gave rise to the multiple alpha-Hsps present in most organisms.

  • genealogy of the α crystallin small heat shock protein superfamily
    International Journal of Biological Macromolecules, 1998
    Co-Authors: W.w. De Jong, Gertjan Caspers, Jack A M Leunissen
    Abstract:

    Sequences of 40 very diverse representatives of the α-crystallin–small heat-shock protein (α-Hsp) superfamily are compared. Their characteristic C-terminal `α-crystallin domain' of 80–100 residues contains short consensus sequences that are highly conserved from prokaryotes to Eukaryotes. There are, in addition, some positions that clearly distinguish animal from non-animal α-Hsps. The α-crystallin domain is predicted to consist of two hydrophobic β-sheet motifs, separated by a hydrophilic region which is variable in length. Combination of a conserved α-crystallin domain with a variable N-terminal domain and C-terminal extension probably modulates the properties of the various α-Hsps as stress-protective and structural oligomeric proteins. Phylogeny reconstruction indicates that multiple α-Hsps were already present in the last common ancestor of pro- and Eukaryotes. It is suggested that during Eukaryote Evolution, animal and non-animal α-Hsps originated from different ancestral gene copies. Repeated gene duplications gave rise to the multiple α-Hsps present in most organisms.

Richard Cordaux - One of the best experts on this subject based on the ideXlab platform.

  • population genomics supports baculoviruses as vectors of horizontal transfer of insect transposons
    Nature Communications, 2014
    Co-Authors: Clement Gilbert, Aurélien Chateigner, Lise Ernenwein, Valérie Barbe, Annie Bézier, Elisabeth A Herniou, Richard Cordaux
    Abstract:

    Horizontal transfer (HT) of DNA is an important factor shaping Eukaryote Evolution. Although several hundreds of Eukaryote-to-Eukaryote HTs of transposable elements (TEs) have been reported, the vectors underlying these transfers remain elusive. Here, we show that multiple copies of two TEs from the cabbage looper (Trichoplusia ni) transposed in vivo into genomes of the baculovirus Autographa californica multiple nucleopolyhedrovirus (AcMNPV) during caterpillar infection. We further demonstrate that both TEs underwent recent HT between several sympatric moth species (T. ni, Manduca sexta, Helicoverpa spp.) showing different degrees of susceptibility to AcMNPV. Based on two independent population genomics data sets (reaching a total coverage >330,000X), we report a frequency of one moth TE in ~8,500 AcMNPV genomes. Together, our results provide strong support for the role of viruses as vectors of TE HT between animals, and they call for a systematic evaluation of the frequency and impact of virus-mediated HT on the Evolution of host genomes. Horizontal transfer of DNA is common among Eukaryotes but the vectors involved remain elusive. Here, Gilbert et al. show high frequency of in vivotransposition from the cabbage looper moth into genomes of a baculovirus, suggesting that viruses can act as vectors of horizontal transfer between animals.

  • horizontal transfer and Evolution of prokaryote transposable elements in Eukaryotes
    Genome Biology and Evolution, 2013
    Co-Authors: Clement Gilbert, Richard Cordaux
    Abstract:

    Horizontal transfer (HT) of transposable elements (TEs) plays a key role in prokaryotic Evolution, and mounting evidence suggests that it has also had an important impact on eukaryotic Evolution. Although many prokaryote-to-prokaryote and Eukaryote-to-Eukaryote HTs of TEs have been characterized, only few cases have been reported between prokaryotes and Eukaryotes. Here, we carried out a comprehensive search for all major groups of prokaryotic insertion sequences (ISs) in 430 Eukaryote genomes. We uncovered a total of 80 sequences, all deriving from the IS607 family, integrated in the genomes of 14 Eukaryote species belonging to four distinct phyla (Amoebozoa, Ascomycetes, Basidiomycetes, and Stramenopiles). Given that Eukaryote IS607-like sequences are most closely related to cyanobacterial IS607 and that their phylogeny is incongruent with that of their hosts, we conclude that the presence of IS607-like sequences in eukaryotic genomes is the result of several HT events. Selection analyses further suggest that our ability to detect these prokaryote TEs today in Eukaryotes is because HT of these sequences occurred recently and/or some IS607 elements were domesticated after HT, giving rise to new Eukaryote genes. Supporting the recent age of some of these HTs, we uncovered intact full-length, potentially active IS607 copies in the amoeba Acanthamoeba castellani. Overall, our study shows that prokaryote-to-Eukaryote HT of TEs occurred at relatively low frequency during recent Eukaryote Evolution and it sets IS607 as the most widespread TE (being present in prokaryotes, Eukaryotes, and viruses).

Zhonghe Zhai - One of the best experts on this subject based on the ideXlab platform.

  • identification of the nuclear matrix and chromosome scaffold in dinoflagellate crypthecodinium cohnii
    Cell Research, 1992
    Co-Authors: Congmei Zeng, Jingyan Li, Zhonghe Zhai
    Abstract:

    Dinoflagellate is one of the primitive Eukaryotes, whose nucleus may represent one of the transition stages from prokaryotic nucleoid to typical eukaryotic nucleus. Using selective extraction together with embeddment−free section and whole mount electron microscopy, a delicate nuclear matrix filament network was shown, for the first time, in dinoflagellate Crypthecodinium cohnii nucleus. Chromosome residues are connected with nuclear matrix filaments to form a complete network spreading over the nucleus. Moreover, we demonstrated that the dinoflagellate chromosome retains a protein scaffold after the depletion of DNA and soluble proteins. This scaffold preserves the characteristic morphology of the chromosome. Two dimensional electrophoreses indicated that the nuclear matrix and chromosome scaffold are mainly composed of acidic proteins. Our results demonstrated that a framework similar to the nuclear matrix and chromosome scaffold in mammalian cells appears in this primitive Eukaryote,suggesting that these structures may have been originated from the early stages of Eukaryote Evolution.