scholarly journals Two Pathogenic Gene Mutations Identified Associating with Congenital Cataract and Iris Coloboma Respectively in a Chinese Family

2020 ◽  
Vol 2020 ◽  
pp. 1-9
Author(s):  
Bin Li ◽  
Bin Lu ◽  
Xuewen Guo ◽  
Shenghui Hu ◽  
Guihu Zhao ◽  
...  
Keyword(s):  
Congenital Cataract ◽  
Three Dimensional ◽  
Gene Mutations ◽  
Dimensional Structure ◽  
Chinese Family ◽  
Control Group ◽  
Three Dimensional Structure ◽  
Han Ethnicity ◽  
The Family ◽  
The Impact

Purpose. To screen out pathogenic genes in a Chinese family with congenital cataract and iris coloboma. Material and Methods. A three-generation family with congenital cataract and iris coloboma from a Han ethnicity was recruited. DNA was extracted from peripheral blood samples collected from all individuals in the family. Whole exon sequencing was employed for screening the disease-causing gene mutations in the proband, and Sanger sequencing was used for other members of the family and a control group of 500 healthy individuals. Bioinformatics analysis and three-dimensional structure predictions were used to predict the impact of amino acid changes on protein structure and function. Results. The candidate genes of cataract and iris coloboma were successfully screened out. A heterozygote mutation, CRYGD c.70C>A (p.P24T), was identified as cosegregating with congenital cataracts, while another heterozygous mutation, WFS1 c.1514G>C (p.C505S), which had not been reported previously, cosegregated with congenital iris coloboma. Bioinformatic analyses and three-dimensional structure prediction proved that the three-dimensional structures of WFS1 p.C505S and CRYGD p.P24T changed markedly and may contribute significantly to iris coloboma and congenital cataract, respectively. Conclusions. We report a novel mutation, WFS1 p.C505S, and a known mutation, CRYGD p.P24T, that cosegregate with iris coloboma and congenital cataract, respectively, in a Chinese family. This is the first time the association of WFS1 p.C505S with iris coloboma has been demonstrated, although CRYGD p.P24T has been widely reported as being associated with congenital cataract, especially in the Eastern Asian population. These findings may have future therapeutic benefit for the diagnosis of iris coloboma and congenital cataract. The results may also be relevant in further studies aiming to investigate the molecular pathogenesis of iris coloboma and congenital cataract.

Structural Differences in the Tracheal Tapetum of Diurnal Butterflies

1979 ◽  
Vol 34 (3-4) ◽  
pp. 284-287 ◽  
Author(s):  
Willi A. Ribi
Keyword(s):  
Three Dimensional ◽  
Dimensional Structure ◽  
Three Dimensional Structure ◽  
Receptor Cells ◽  
Screening Pigment ◽  
The Family ◽  
Tapetum Lucidum ◽  
Structural Differences ◽  
First Results ◽  
Physiological Differences

Abstract The three-dimensional structure of the tracheal tapetum lucidum, its reflection properties and the resulting eye glow hue were studied in members of the diurnal butterfly families Pieridae, Nymphalidae, Satyridae and Lycaenidae. Two main groups of tapeta can be distinguished by structural and physiological differences. Whereas in pierids the main tracheal trunk at the bottom of the rhabdom bifurcates into two side branches before bifurcating again more distally, the tracheal trunk in the members of the family Nymphalidae, Satyridae and Lycaenidae investigated first divides into four side brandies. A second bifurcation shortly after the first results in eight subbranches which are regularly arranged between adjoining receptor cells. The broad banded reflection colour from incidently illuminated tapetal structures (at the level of the first bifurcation) varies between and within families but does not change significantly within the same eye. Whereas in nymphalids, satyrids and lycaenids the eye glow hue corresponds with the colour of the tapetal reflection, in pierids it is dominated by the coloured receptor screening pigment.

scholarly journals Novel biological implication of a strictly monomorphic GCC repeat in the human PRKACB gene

2021 ◽  
Author(s):  
Safoura Khamse ◽  
Zahra Jafarian ◽  
Ali Bozorgmehr ◽  
Mostafa Tavakoli ◽  
Hossein Afshar Iranian ◽  
...  
Keyword(s):  
Late Onset ◽  
Human Subjects ◽  
Three Dimensional ◽  
Dna Structure ◽  
Dimensional Structure ◽  
Protein Coding ◽  
Three Dimensional Structure ◽  
Significant Divergence ◽  
The Impact ◽  
The Brain

Abstract Across human protein-coding genes, PRKACB (Protein Kinase CAMP-Activated Catalytic Subunit Beta) contains one of the longest GCC-repeats, and is predominantly expressed in the brain. Here we studied this STR in 300 human subjects, consisting of late-onset neurocognitive disorder (NCD) (N = 150) and controls (N = 150). We also studied the impact of this STR on the three-dimensional structure of DNA. While the PRKACB GCC-STR was strictly monomorphic at 7-repeats, we detected two 7/8 genotypes only in the NCD group. In comparison to all other lengths, (GCC)7 had the least effect on the three-dimensional structure of DNA, evidenced by minimal divergence between 0 and 7-repeats (divergence score = 0.04) and significant divergence between 0 and 8 repeats (divergence score = 0.50). A similar inert effect to the GCC-repeat was not detected in other classes of STRs such as GA and CA repeats. In conclusion, we report monomorphism of an exceptionally long GCC repeat in the PRKACB gene in human, its inert effect on DNA structure, and divergence in two cases of late-onset NCD. This is the first indication of natural selection for an exceptionally long monomorphic GCC-repeat, which probably evolved to function as an “epigenetic knob”, without changing the regional DNA structure.

scholarly journals The Three-Dimensional Structure of Giardia lamblia Virus and its Comparison to Other Members of the Family Totiviridae

2013 ◽  
Vol 19 (S2) ◽  
pp. 88-89
Author(s):  
M.E. Janssen ◽  
K.N. Parent ◽  
Y. Takagi ◽  
M.L. Nibert ◽  
T.S. Baker
Keyword(s):  
Giardia Lamblia ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Three Dimensional Structure ◽  
The Family

Extended abstract of a paper presented at Microscopy and Microanalysis 2013 in Indianapolis, Indiana, USA, August 4 – August 8, 2013.

scholarly journals Frequent SLC12A3 mutations in Chinese Gitelman syndrome patients: structure and function disorder

2021 ◽  
Author(s):  
Lanping Jiang ◽  
Xiaoyan Peng ◽  
Bingbin Zhao ◽  
Lei Zhang ◽  
Lubin Xu ◽  
...  
Keyword(s):  
Three Dimensional ◽  
Gene Mutations ◽  
Dimensional Structure ◽  
Novel Mutations ◽  
Three Dimensional Structure ◽  
Slc12a3 Gene ◽  
Uptake Experiment ◽  
Frequent Mutations ◽  
22Na Uptake

Purposes: This study was conducted to identify the frequent mutations from reported Chinese Gitelman syndrome (GS) patients, to predict three-dimensional structure change of human Na-Cl co-transporter (hNCC), and to test the activity of these mutations and some novel mutations in vitro and in vivo. Methods: SLC12A3 gene mutations in Chinese GS patients previously reported in the PubMed, CNKI and Wanfang database were summarized. Predicted configurations of wild type (WT) and mutant proteins were achieved using the I-TASSER workplace. Six missense mutations (T60M, L215F, D486N, N534K, Q617R and R928C) were generated by site-directed mutagenesis. 22Na+ uptake experiment was carried out in the Xenopus laevis oocyte expression system. 35 GS patients and 20 healthy volunteers underwent the thiazide test. Results: T60M, T163M，D486N, R913Q, R928C and R959 frameshift were frequent SLC12A3 gene mutations (mutated frequency >3%) in 310 Chinese GS families. The protein’s three-dimensional structure was predicted to be altered in all mutations. Compared with WT hNCC, the thiazide-sensitive 22Na+ uptake was significantly diminished for all 6 mutations: T60M 22±9.2%, R928C 29±12%, L215F 38±14%, N534K 41±15.5%, Q617R 63±22.1% and D486N 77±20.4%. In thiazide test, the net increase in chloride fractional excretion in 20 healthy controls was significantly higher than GS patients with or without T60M or D486N mutations. Conclusions: Frequent mutations (T60M, D486N, R928C) and novel mutations (L215F, N534K and Q617R) lead to protein structure alternation and protein dysfunction verified by 22Na+ uptake experiment in vitro and thiazide test on patients.

Contrasting the temporal dynamics of stand structure in even- and uneven-sized Picea abies dominated stands

2011 ◽  
Vol 41 (2) ◽  
pp. 289-299 ◽  
Author(s):  
Eric K. Zenner ◽  
Erkki Lähde ◽  
Olavi Laiho
Keyword(s):  
Temporal Dynamics ◽  
Three Dimensional ◽  
Tree Size ◽  
Dimensional Structure ◽  
Diameter Distribution ◽  
Structural Development ◽  
Three Dimensional Structure ◽  
Single Tree ◽  
Single Tree Selection ◽  
The Impact

Although proposed as a means of increasing structural diversity in managed forests, the impact of single-tree selection on the temporal dynamics of three-dimensional structure has not been previously evaluated. Forest structural development in Picea-dominated stands was contrasted over 15 years in stem-mapped randomized plots in southern Finland that underwent either low thinning (creating the even-sized (ES) structure of a bell-shaped diameter distribution) or single-tree selection (maintaining the uneven-sized (UES) structure of a reverse-J-shaped distribution) through multiple harvest entries. Structure was quantified with nonspatial stand attributes (e.g., density) and indices that quantify spatially explicit relationships among neighboring trees (e.g., structural complexity index (SCI)). Over time, three-dimensional structure reflected differential tree growth and mortality, resulting in minor changes in tree composition, spatial pattern, and tree size differentiation and somewhat greater changes in the SCI. The third harvest entry simplified the forest structure in both structure types. However, structural metrics such as the variability of tree diameters, tree size differentiation, and the SCI recovered to preharvest levels within 2–4 years in UES plots, whereas no recovery was seen in the ES structure type. Single-tree selection was demonstrated to perpetuate the uneven-sized structure associated with natural nonpyrogenic Picea-dominated forests.

Modeling the impact of point mutations on the stability of proteins

2020 ◽  
Vol 18 (04) ◽  
pp. 2050019
Author(s):  
K. G. Kulikov ◽  
T. V. Koshlan
Keyword(s):  
Protein Interactions ◽  
Protein Complexes ◽  
Three Dimensional ◽  
Point Mutations ◽  
Dimensional Structure ◽  
Amino Acid Residues ◽  
Three Dimensional Structure ◽  
The Stability ◽  
The Impact ◽  
Proven Theorem

A new method has been introduced which allows us to determine the stability of protein complexes with point changes of amino acid residues that also take into account the three-dimensional structure of the complex. This formulated and proven theorem is aimed at determining the criterion for the stability of protein molecules. The algorithm and software package were developed for analyzing protein interactions, taking into account their three-dimensional structure from the PDB database.

scholarly journals Three-dimensional structure of a thermophilic family GH11 xylanase fromThermobifida fusca

2012 ◽  
Vol 68 (2) ◽  
pp. 141-144 ◽  
Author(s):  
Alicia Lammerts van Bueren ◽  
Suzie Otani ◽  
Esben P. Friis ◽  
Keith S. Wilson ◽  
Gideon J. Davies
Keyword(s):  
Hydrogen Bonds ◽  
Three Dimensional ◽  
Structural Features ◽  
Dimensional Structure ◽  
Amino Acid Sequence Level ◽  
Thermostable Enzymes ◽  
Solvent Interactions ◽  
Three Dimensional Structure ◽  
The Family ◽  
Moderate Thermophile

Thermostable enzymes employ various structural features dictated at the amino-acid sequence level that allow them to maintain their integrity at higher temperatures. Many hypotheses as to the nature of thermal stability have been proposed, including optimized core hydrophobicity and an increase in charged surface residues to enhance polar solvent interactions for solubility. Here, the three-dimensional structure of the family GH11 xylanase from the moderate thermophileThermobifida fuscain its trapped covalent glycosyl-enzyme intermediate complex is presented. Interactions with the bound ligand show fewer direct hydrogen bonds from ligand to protein than observed in previous complexes from other species and imply that binding of the xylan substrate involves several water-mediated hydrogen bonds.

Folding of the td pre-RNA with the help of the RNA chaperone StpA

2002 ◽  
Vol 30 (6) ◽  
pp. 1175-1180 ◽  
Author(s):  
O. Mayer ◽  
C. Waldsich ◽  
R. Grossberger ◽  
R. Schroeder
Keyword(s):  
Conformational Changes ◽  
Three Dimensional ◽  
Group I Intron ◽  
Dimensional Structure ◽  
Rna Chaperone ◽  
Three Dimensional Structure ◽  
Group I ◽  
The Impact

The td group I intron is inserted in the reading frame of the thymidylate synthase gene, which is mainly devoid of structural elements. In vivo, translation of the pre-mRNA is required for efficient folding of the intron into its splicing-competent structure. The ribosome probably resolves exon-intron interactions that interfere with splicing. Uncoupling splicing from translation, by introducing a non-sense codon into the upstream exon, reduces the splicing efficiency of the mutant pre-mRNA. Alternatively to the ribosome, co-expression of genes that encode proteins with RNA chaperone activity promote folding of the td pre-mRNA in vivo. These proteins also efficiently accelerate folding of the td pre-mRNA in vitro. In order to understand the mechanism of action of RNA chaperones, we probed the impact of the RNA chaperone StpA on the structure of the td intron in vivo and compared it with that of the well characterized Cyt-18 protein, which is a group-I-intron-specific splicing factor. We found that the two proteins have opposite effects on the structure of the td intron. While StpA loosens the three-dimensional structure, Cyt-18 tightens it up. Furthermore, mutations that destabilize the intron structure render the mutants sensitive to StpA, whereas splicing of these mutants is rescued by Cyt-18. Our results provide direct evidence for protein-induced conformational changes within a catalytic RNA in vivo. Whereas StpA resolves tertiary contacts enabling the RNA to refold, Cyt-18 contributes to the stabilization of the native three-dimensional structure.

The Three-dimensional structure of frozen-hydrated nudaurelia capensis β virus

1987 ◽  
Vol 45 ◽  
pp. 650-651
Author(s):  
N. H. Olson ◽  
T. S. Baker ◽  
Wu Bo Mu ◽  
J. E. Johnson ◽  
D. A. Hendry
Keyword(s):  
South African ◽  
Rna Virus ◽  
Carbon Film ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Electron Dose ◽  
Total Electron ◽  
Three Dimensional Structure ◽  
Negative Stain ◽  
Dimensional Reconstruction

Nudaurelia capensis β virus (NβV) is an RNA virus of the South African Pine Emperor moth, Nudaurelia cytherea capensis (Lepidoptera: Saturniidae). The NβV capsid is a T = 4 icosahedron that contains 60T = 240 subunits of the coat protein (Mr = 61,000). A three-dimensional reconstruction of the NβV capsid was previously computed from visions embedded in negative stain suspended over holes in a carbon film. We have re-examined the three-dimensional structure of NβV, using cryo-microscopy to examine the native, unstained structure of the virion and to provide a initial phasing model for high-resolution x-ray crystallographic studiesNβV was purified and prepared for cryo-microscopy as described. Micrographs were recorded ∼1 - 2 μm underfocus at a magnification of 49,000X with a total electron dose of about 1800 e-/nm2.

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