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At least 1,297 records · Page 72Linked to original sources
PubMed2004

Sequence variability in the structural protein-encoding region of foot-and-mouth disease virus serotype Asia1 field isolates.

A total of 30 field isolates of foot-and-mouth disease virus (FMDV) serotype Asia1 belonging to two different lineages and five isolates belonging to a divergent group as delineated earlier in 1D (encodingVP1 protein) gene-based phylogeny were sequenced in the structural protein (P1) coding region. Phylogenetic comparison of these isolates along with some of the published exotic sequences revealed the presence of five different lineages around the world. Similar grouping pattern was observed for the P1 region and 1D gene-based phylogeny, where the Indian isolates were clustered in two genetic lineages. The recently identified divergent group of virus falls into a separate sub-cluster. Similar grouping was also observed in L gene-based phylogeny. Comparison of amino acid sequences identified lineage-specific signature residues in all the structural proteins. Comparison of Asia1 field isolates at the identified key residues of other FMD viruses involved in the formation of the heparan sulfate-binding ligand confirmed many of them to be conserved and the presence of VP3(56) Arg suggested their cell culture adaptation. Although a considerable genetic variation was observed among the isolates of present study, all of them tested in micro-neutralization test were serologically related to the vaccine strain.

Amino Acid Sequence↗
PubMed1979

"The diencephalon of Ptilocercus lowii (pen-tailed tree-shrew)".

The pen-tailed tree-shrew (Ptilocercus lowii) has been regarded by Le Gros Clark (1926), and Martin (1968) to possess more primitive morphological and to a certain extent, neuro-anatomical characteristics than the other tree-shrew species belonging to the sub-family Tupaiinae. Investigations have been carried out on the diencephalon of Ptilocercus lowii which has not been completely done by Le Gros Clark and other workers since 1926, to find out whether the diencephalon has actually undegone any phylogenetic changes that should be more advanced than those of the Insectivora or remain more primitive than that of the Tupaiinae. The diencephalic structure that show the most significant phylogenetic features which differe Ptilocerecus from Tupaia are observed in the anterior, dorsolateral and ventrolateral thalamic groups, and the geniculate bodies. The nucleus anteroventralis is, by comparison, much smaller and poorly differentiated from the nucleus anteromedialis. The nucleus anterodorsalis is also comparably large and does not reach the dorsal surface of the thalamus as it does in the primates. The midline nuclei do not show any significant differences, except the notably larger size of nucleus parataenialis in Ptilocercus. The nucleus mediodoralis is small and indifferentiated although it does show some incipient signs of cellular differentiation. The nucleus centralis lateralis is well developed; its inferior (ventral) part is larger than its superior part which is the better developed of the two parts in the tupaiids and primates. The nucleus centrum medianum appears to be very small and forms only a lateral extension of the nucleus parafascicularis. The ventrolateral thalamic group basically consists of nuclei ventrales anterior, lateralis and posterior without intermediate or transitional zones as found in Tupaia and Primates. The nucleus pretectalis is the largest and the best developed of all the elements of the posterior thalamic nuclear group. The lateral geniculate nucleus is not differentiated into laminae like that in Tupaia and Primates; it is merely a homogeneous structure that appears to be smaller in size that the pregeniculate and medial geniculate nuclei. The medial geniculate nucleus is large in proportional size of the whole thalamus and appears to be well differentiated cellularly into several small parts. No remarkable changes are noted in the epithalamus, subthalamus and hypothalamus. However, the nucleus ventromedialis appears to be the most outstanding structure in the infundibular region of the hypothalamus. The mammillary region is of a simpler construction in Ptilocercus than in Tupaia; it does not protrude from the ventral surface of the hypothalamus. In the light of these findings, the phyletic status of Ptilocercus in the family Tupaiidae is discussed.

Animals↗
PubMed1998

The presence of modified nucleotides is required for cloverleaf folding of a human mitochondrial tRNA.

Direct sequencing of human mitochondrial tRNALysshows the absence of editing and the occurrence of six modified nucleotides (m1A9, m2G10, Psi27, Psi28 and hypermodified nucleotides at positions U34 and A37). This tRNA folds into the expected cloverleaf, as confirmed by structural probing with nucleases. The solution structure of the corresponding in vitro transcript unexpectedly does not fold into a cloverleaf but into an extended bulged hairpin. This non-canonical fold, established according to the reactivity to a large set of chemical and enzymatic probes, includes a 10 bp aminoacyl acceptor stem (the canonical 7 bp and 3 new pairs between residues 8-10 and 65-63), a 13 nt large loop and an anticodon-like domain. It is concluded that modified nucleotides have a predominant role in canonical folding of human mitochondrial tRNALys. Phylogenetic comparisons as well as structural probing of selected in vitro transcribed variants argue in favor of a major contribution of m1A9 in this process.

Cloning, Organism↗
PubMed2006

Operational principles of neurocognitive networks.

Large-scale neural networks are thought to be an essential substrate for the implementation of cognitive function by the brain. If so, then a thorough understanding of cognition is not possible without knowledge of how the large-scale neural networks of cognition (neurocognitive networks) operate. Of necessity, such understanding requires insight into structural, functional, and dynamical aspects of network operation, the intimate interweaving of which may be responsible for the intricacies of cognition. Knowledge of anatomical structure is basic to understanding how neurocognitive networks operate. Phylogenetically and ontogenetically determined patterns of synaptic connectivity form a structural network of brain areas, allowing communication between widely distributed collections of areas. The function of neurocognitive networks depends on selective activation of anatomically linked cortical and subcortical areas in a wide variety of configurations. Large-scale functional networks provide the cooperative processing which gives expression to cognitive function. The dynamics of neurocognitive network function relates to the evolving patterns of interacting brain areas that express cognitive function in real time. This article considers the proposition that a basic similarity of the structural, functional, and dynamical features of all neurocognitive networks in the brain causes them to function according to common operational principles. The formation of neural context through the coordinated mutual constraint of multiple interacting cortical areas, is considered as a guiding principle underlying all cognitive functions. Increasing knowledge of the operational principles of neurocognitive networks is likely to promote the advancement of cognitive theories, and to seed strategies for the enhancement of cognitive abilities.

Animals↗
PubMed2005

[Phylogenetic diversity analyse of rumen bacteria using culture independent method].

Culture independent method was used to study the diversity of rumen bacteria. Molecular diversity of rumen bacteria was analyzed by PCR amplification and sequencing of 16S rDNA clone libraries prepared from the rumen content of Holstein cows. The total DNA directly extracted from rumen fluid was used as PCR template. Bacteria universal primer 27F and 1492R was used as primer. Random clones, containing almost full size 16S rDNA sequences (about 1.5 kb long), were sequenced and subjected to an on line similarity search. The 16S rDNA sequence analysis indicated that more than half of the sequences belonged to the not-yet-cultured groups. The 16S rDNA similarity levels with cultured species was less than 90%. The bacterial community structure was also revealed by phylogenetic tree of known sequences and selected sequence. In the library from the rumen fluid, the sequences were mainly affiliated with the following major phyla: low G + C Gram-positive bacteria, Cytophaga-Flexibacter-Bacteroides, and the remaining sequences were placed within not-yet-uncultured groups that had an uncertain affiliation. These several sequences are likely to represent novel taxonomic groupings. The nucleotide sequences have been submitted to the GenBank/EMBL /DDBJ databases under accession numbers AY986777-AY986791.

Animals↗
PubMed1995

Identification and characterization of T-cell antigen receptor-related genes in phylogenetically diverse vertebrate species.

Characterization of the structure, multiplicity, organization, and cell lineage-specific expression of T-cell receptor (TCR) genes of nonmammalian vertebrate species is central to the understanding of the evolutionary origins of rearranging genes of the vertebrate immune system. We recently described a polymerase chain reaction (PCR) strategy that relies on short sequence similarities shared by nearly all vertebrate TCR and immunoglobulin (Ig) variable (V) regions and have used this approach to isolate a TCR beta (TCRB) homolog from a cartilaginous fish. Using these short PCR products as probes in spleen cDNA and genomic libraries, we were able to isolate a variety of unique TCR and TCR-like genes. Here we report the identification and characterization of a chicken TCR gamma (TCRG) homolog, apparent Xenopus and pufferfish TCR alpha (TCRA) homologs, and two horned shark TCR delta (TCRD)-like genes. In addition, we have identified what could be a novel representative of the Ig gene superfamily in the pufferfish. This method of using short, minimally degenerate PCR primers should speed progress in the phylogenetic investigations of the TCR and related genes and lend important insights into both the origins and functions of these unique gene systems.

Amino Acid Sequence↗
PubMedDate not supplied

Signal, noise, and reliability in molecular phylogenetic analyses.

DNA sequences and other molecular data compared among organisms may contain phylogenetic signal, or they may be randomized with respect to phylogenetic history. Some method is needed to distinguish phylogenetic signal from random noise to avoid analysis of data that have been randomized with respect to the historical relationships of the taxa being compared. We analyzed 8,000 random data matrices consisting of 10-500 binary or four-state characters and 5-25 taxa to study several options for detecting signal in systematic data bases. Analysis of random data often yields a single most-parsimonious tree, especially if the number of characters examined is large and the number of taxa examined is small (both often true in molecular studies). The most-parsimonious tree inferred from random data may also be considerably shorter than the second-best alternative. The distribution of tree lengths of all tree topologies (or a random sample thereof) provides a sensitive measure of phylogenetic signal: data matrices with phylogenetic signal produce tree-length distributions that are strongly skewed to the left, whereas those composed of random noise are closer to symmetrical. In simulations of phylogeny with varying rates of mutation (up to levels that produce random variation among taxa), the skewness of tree-length distributions is closely related to the success of parsimony in finding the true phylogeny. Tables of critical values of a skewness test statistic, g1, are provided for binary and four-state characters for 10-500 characters and 5-25 taxa. These tables can be used in a rapid and efficient test for significant structure in data matrices for phylogenetic analysis.

Animals↗
PubMed2026

Recent gene duplication and structural remodeling drive rapid lineage-specific gene family evolution in plants.

Gene duplication promotes the generation of novel gene functions and trait diversity across species. Here, we present DupHIST, a computational pipeline that reconstructs the hierarchical timing of gene duplications by integrating maximum likelihood (ML)-based phylogeny with substitution-derived timing via statistical smoothing. Applied to over 4.5 million genes from 114 plant genomes, we successfully inferred duplication histories across nearly 130,000 orthogroups. This large-scale analysis showed that 53.0% of genes arose from recent, lineage-specific duplications, with high concentrations in particular multi-copy families. Among these, NLR, C48, and P450 families exemplified how recently duplicated genes undergo rapid stepwise structural remodeling. This process was primarily driven by small-scale mutations, including insertions, deletions, and frameshifts, that rapidly accumulated shortly after duplication. By resolving the precise duplication order, we reconstructed these architectural changes, thereby enabling both the inference of putative ancestral structures and the exploration of functional diversification arising from structural remodeling. Structure-based clustering further uncovered that recently duplicated, uncharacterized genes retain core domain structures resembling known functional proteins even across phylogenetically distant species lacking sequence homology. Our findings reveal that recent gene duplications and subsequent structural remodeling represent a widespread and lineage-specific force driving rapid diversification of gene families in plants.

Gene duplication history↗
PubMed1986

Identification of dynamic sequences in the central domain of 7SL RNA.

The human 7SL RNA component of the signal recognition particle can be separated into four major conformers by nondenaturing polyacrylamide gel electrophoresis. We have investigated what sequences give 7SL RNA the property to exist in different conformations. The human 7SL gene 7L30.1 was mutagenized using the random linker insertion approach and twelve mutant genes carrying alterations in the central domain of 7SL RNA were characterized. Mutant RNAs were produced by in vitro transcription of the various templates and their electrophoretic behaviour was determined. Bases between positions 98 and 133 as well as 206 and 251 proved to be necessary for the 7SL RNA to be able to exist in alternative conformations, while changes at the positions 85 to 97, 144 to 166 and 252 to 266 did not abolish this property. The dynamic sequences are located in the "central T" in the secondary structure of the 7SL RNA. They are phylogenetically conserved and include bases which are homologeous to 5S ribosomal RNA. A dynamic core structure composed of the dynamic parts of the 7SL RNA is suggested. An attempt was made to define the different conformers present in the wild-type 7SL RNA. These alternative configurations could play a functional role during the initial stage of protein translocation across the membrane of the endoplasmic reticulum.

Base Sequence↗
PubMed2002

The pattern of amino acid replacements in alpha/beta-barrels.

The determinants of site-to-site variability in the rate of amino acid replacement in alpha/beta-barrel enzyme structures are investigated. Of 125 available alpha/beta-barrel structures, only 25 meet a variety of phylogenetic and statistical criteria necessary to ensure sufficient data for reliable analysis. These 25 enzyme structures (from a wide variety of taxa with diverse lifestyles in diverse habitats) differ greatly in size, number, and topology of domains in addition to the alpha/beta-barrel, quaternary structure, metabolic role, reaction catalyzed, presence of prosthetic groups, regulatory mechanisms, use of cofactors, and catalytic mechanisms. Yet, with the exception of ribulose-1,5-bisphosphate carboxylase, all structures have similar frequency distributions of amino acid replacement rates. Hence, site-specific variability in rates of evolution is largely independent of differences in biology, biochemistry, and molecular structure. A correlation between site-specific rate variation and (1) distance from the active site, (2) solvent accessibility, and (3) treating glycines in unusual main-chain conformations as a separate class, explains approximately half the causal variation. Secondary structure exerts little influence on the pattern and distribution of replacements. Additional domains and subunits, side-chain hydrogen bonds, unusual side-chain rotamers, nonplanar peptide bonds, strained main-chain conformations, and buried hydrophilic-charged residues contribute little to variability among sites because they are rare. Nonlinear models do not improve the fits. In several enzymes, deviations from the typical pattern of replacements suggest the possible action of natural selection. A statistical analysis shows that, in all cases, much of the remaining unexplained variation is not attributable to chance and that other, as yet unidentified, causal relations must exist.

Amino Acid Sequence↗
PubMedDate not supplied

Genetic variation of southern hemisphere fur seals (Arctocephalus spp.): investigation of population structure and species identity.

We have examined phylogenetic and geographic patterns of variation in the mitochondrial cytochrome b gene of Southern Hemisphere fur seals (Arctocephalus spp.). Our survey of 106 individuals from four putative species reveals three distinct patterns of variation reflecting ancient, recent historic, and contemporary gene flow. For the combined samples of Subantarctic (Arctocephalus tropicalis) and Antarctic (Arctocephalus gazella) fur seals, we find low levels of sequence diversity and reciprocal paraphyly of hapiotypes (where representative haplotypes of a species are found to occur infrequently in another species and vice versa). For the Australian and Cape fur seal subspecies (Arctocephalus pusillus doriferus and A. p. pusillus, respectively), we find low levels of sequence diversity but significant differences in the regional distribution of haplotypes that are consistent with, but not conclusive of, the current subspecies definition based on nonmolecular data. For the New Zealand fur seal (Arctocephalus forsteri), we find high levels of average sequence diversity because of the survival of two divergent lineages of mitochondrial hapiotypes with differences approaching that found in interspecific comparisons of other mammals. The two divergent clades are distributed sympatrically in some regions, but the overall geographic structure of the variation is significant across the range of this species. These new molecular data are inconsistent with current taxonomic definitions of species within the Southern Hemisphere fur seals and argue for reevaluation of these "species" definitions. For management purposes, the definition of evolutionarily significant units (Ryder 1986) and genetic management units (Moritz 1994) in relation to these species may also be evaluated in light of this molecular genetic information.

Animals↗
PubMed1993

Evolution of protein complexity: the blue copper-containing oxidases and related proteins.

The blue copper proteins and their relatives have been compared by sequence alignments, by comparison of three-dimensional structures, and by construction of phylogenetic trees. The group contains proteins varying in size from 100 residues to over 2,300 residues in a single chain, containing from zero to nine copper atoms, and with a broad variation in function ranging from electron carrier proteins and oxidases to the blood coagulation factors V and VIII. Difference matrices show the sequence difference to be over 90% for many pairs in the group, yet alignment scores and other evidence suggest that they all evolved from a common ancestor. We have attempted to delineate how this evolution took place and in particular to define the mechanisms by which these proteins acquired an ever-increasing complexity in structure and function. We find evidence for six such mechanisms in this group of proteins: domain enlargement, in which a single domain increases in size from about 100 residues up to 210; domain duplication, which allows for a size increase from about 170 to about 1,000 residues; segment elongation, in which a small segment undergoes multiple successive duplications that can increase the chain size 50-fold; domain recruitment, in which a domain coded elsewhere in the genome is added on to the peptide chain; subunit formation, to form multisubunit proteins; and glycosylation, which in some cases doubles the size of the protein molecule. Size increase allows for the evolution of new catalytic properties, in particular the oxidase function, and for the formation of coagulation factors with multiple interaction sites and regulatory properties. The blood coagulation system is examined as an example in which a system of interacting proteins evolved by successive duplications of larger parts of the genome. The evolution of size, functionality, and diversity is compared with the general question of increase in size and complexity in biology.

Amino Acid Sequence↗
PubMed2006

Predicting genes for orphan metabolic activities using phylogenetic profiles.

Homology-based methods fail to assign genes to many metabolic activities present in sequenced organisms. To suggest genes for these orphan activities we developed a novel method that efficiently combines local structure of a metabolic network with phylogenetic profiles. We validated our method using known metabolic genes in Saccharomyces cerevisiae and Escherichia coli. We show that our method should be easily transferable to other organisms, and that it is robust to errors in incomplete metabolic networks.

Databases, Nucleic Acid↗
PubMed2002

The primary structure of hemoglobin D from the Aldabra giant tortoise, Geochelone gigantea.

The complete primary structures of alpha D-2- and beta-globin of hemoglobin D (Hb D) from the Aldabra giant tortoise, Geochelone gigantea, have been constructed by amino acid sequencing analysis in assistance with nucleotide sequencing analysis of PCR fragments amplified using degenerate oligonucleotide primers. Using computer-assisted sequence comparisons, the alpha D-2-globin shared a 92.0% sequence identity versus alpha D-globin of Geochelone carbonaria, a 75.2% versus alpha D-globin of Aves (Rhea americana) and a 62.4% versus alpha A-globin of Hb A expressed in adult red blood cells of Geochelone gigantea. Additionally, judging from their primary structures, an identical beta-globin was common to the two hemoglobin components, Hb A and Hb D. The alpha D-2- and beta-globin genes contained the three-exon and two-intron configurations and showed the characteristic of all functional vertebrate hemoglobin genes except an abnormal GC dinucleotide instead of the invariant GT at the 5' end of the second intron sequence. The introns of alpha D-2-globin gene were both small (224-bp/first intron, 227-bp/second intron) such that they were quite similar to those of adult alpha-type globins; the beta-globin gene has one small intron (approximately 130-bp) and one large intron (approximately 1590-bp). A phylogenetic tree constructed on primary structures of 7 alpha D-globins from Reptilia (4 species of turtles, 2 species of squamates, and 1 species of sphenodontids) and two embryonic alpha-like globins from Aves (Gullus gullus) and Mammals (Homo sapiens) showed the following results: (1) alpha D-globins except those of squamates were clustered, in which Sphenodon punctatus was a closer species to birds than turtles; (2) separation of the alpha A- and alpha D-globin genes occurred approximately 250 million years ago after the embryonic alpha-type globin-genes (pi' and zeta) first split off from the ancestor of alpha-type globin gene family.

Amino Acid Sequence↗
PubMed1988

Complete structure and organization of immunoglobulin heavy chain constant region genes in a phylogenetically primitive vertebrate.

Immunoglobulin (Ig) gene organization in Heterodontus francisci (horned shark), a phylogenetically primitive vertebrate, is unique. Homologous Ig heavy chain variable (VH) and constant region (CH) specific probes were used to screen a spleen cDNA library constructed in lambda gt11. Both secretory (SEC) and transmembrane (TM) cDNA clones were recovered; the latter were identified by a negative selection strategy. The complete sequence of the CH portion of a Heterodontus genomic DNA-lambda clone also was determined. The sequences of the individual CH genes differ from each other in all exons. When compared to mammalian prototypes, similarities in exon and intron organization as well as conservation of sequences involved with differential splicing of SEC and TM mRNA indicate that Heterodontus heavy chain genes are of the mu type, although intron lengths are uniformly longer in Heterodontus. Heterodontus genes are not associated, however, with the family of DNA sequences that have been implicated in heavy chain class switching in mammals. Spleen cDNA library screening and RNA blot analyses indicate that mRNAs encoding TM Ig are exceedingly rare. The relationship between this quantitative difference and the distribution of polyadenylation signal sequences suggests that regulation of Ig gene expression in Heterodontus may be highly dependent on position effects.

Amino Acid Sequence↗
PubMed2000

DNA polymerase of the T4-related bacteriophages.

The DNA polymerase of bacteriophage T4, product of phage gene 43 (gp43), has served as a model replicative DNA polymerase in nucleic acids research for nearly 40 years. The base-selection (polymerase, or Pol) and editing (3'-exonuclease, or Exo) functions of this multifunctional protein, which have counterparts in the replicative polymerases of other organisms, are primary determinants of the high fidelity of DNA synthesis in phage DNA replication. T4 gp43 is considered to be a member of the "B family" of DNA-dependent DNA polymerases (those resembling eukaryotic Pol alpha) because it exhibits striking similarities in primary structure to these enzymes. It has been extensively analyzed at the genetic, physiological, and biochemical levels; however, relationships between the in vivo properties of this enzyme and its physical structure have not always been easy to explain due to a paucity of structural data on the intact molecule. However, gp43 from phage RB69, a phylogenetic relative of T4, was crystallized and its structure solved in a complex with single-stranded DNA occupying the Exo site, as well as in the unliganded form. Analyses with these crystals, and crystals of a T4 gp43 proteolytic fragment harboring the Exo function, are opening new avenues to interpret existing biological and biochemical data on the intact T4 enzyme and are revealing new aspects of the microanatomy of gp43 that can now be explored further for functional significance. We summarize our current understanding of gp43 structure and review the physiological roles of this protein as an essential DNA-binding component of the multiprotein T4 DNA replication complex and as a nucleotide-sequence-specific RNA-binding translational repressor that controls its own biosynthesis and activity in vivo. We also contrast the properties of the T4 DNA replication complex to the functionally analogous complexes of other organisms, particularly Escherichia coli, and point out some of the unanswered questions about gp43 and T4 DNA replication.

Amino Acid Sequence↗
PubMed2001

Phylogenetic analysis of tmRNA genes within a bacterial subgroup reveals a specific structural signature.

Bacterial tmRNA mediates a trans-translation reaction, which permits the recycling of stalled ribosomes and probably also contributes to the regulated expression of a subset of genes. Its action results in the addition of a small number of C-terminal amino acids to protein whose synthesis had stalled and these constitute a proteolytic recognition tag for the degradation of these incompletely synthesized proteins. Previous work has identified pseudoknots and stem-loops that are widely conserved in divergent bacteria. In the present work an alignment of tmRNA gene sequences within 13 beta-proteobacteria reveals an additional sub-structure specific for this bacterial group. This sub-structure is in pseudoknot Pk2, and consists of one to two additional stem-loop(s) capped by stable GNRA tetraloop(s). Three-dimensional models of tmRNA pseudoknot 2 (Pk2) containing various topological versions of the additional sub-structure suggest that the sub-structures likely point away from the core of the RNA, containing both the tRNA and the mRNA domains. A putative tertiary interaction has also been identified.

Base Sequence↗