scholarly journals Transversion Mutation

2020 ◽  
Author(s):  
Keyword(s):  
Transversion Mutation

T26248G-transversion mutation in exon7 of the putative methyltransferase Nsun7 gene causes a change in protein folding associated with reduced sperm motility in asthenospermic men

2015 ◽  
Vol 27 (3) ◽  
pp. 471 ◽  
Author(s):  
Nahid Khosronezhad ◽  
Abasalt Hosseinzadeh Colagar ◽  
Syed Golam Ali Jorsarayi
Keyword(s):  
Protein Folding ◽  
Sperm Motility ◽  
Protein Function ◽  
Direct Sequencing ◽  
Protein Structures ◽  
Single Strand Conformation Polymorphism ◽  
Extraction Methods ◽  
World Health ◽  
Transversion Mutation ◽  
Health Organization

The NOP2/Sun domain family, member 7 (Nsun7) gene, which encodes putative methyltransferase Nsun7, has a role in sperm motility in mice. In humans, this gene is located on chromosome 4 with 12 exons. The aim of the present study was to investigate mutations of exon 7 in the normospermic and asthenospermic men. Semen samples were collected from the Fatemezahra IVF centre (Babol, Iran) and analysed on the basis of World Health Organization (WHO) guidelines using general phenol–chloroform DNA extraction methods. Exon 7 was amplified using Sun7-F and Sun7-R primers. Bands on samples from asthenospermic men that exhibited different patterns of movement on single-strand conformation polymorphism gels compared with normal samples were identified and subjected to sequencing for further identification of possible mutations. Direct sequencing of polymerase chain reaction (PCR) products, along with their analysis, confirmed C26232T-transition and T26248G-transversion mutations in asthenospermic men. Comparison of normal and mutant protein structures of Nsun7 indicated that the amino acid serine was converted to alanine, the structure of the helix, coil and strand was changed, and the protein folding and ligand binding sites were changed in samples from asthenospermic men with a transversion mutation in exon 7, indicating impairment of protein function. Because Nsun7 gene products have a role in sperm motility, if an impairment occurs in exon 7 of this gene, it may lead to infertility. The transversion mutation in exon 7 of the Nsun7 gene can be used as an infertility marker in asthenospermic men.

scholarly journals A novel mutation in the PRPH2 gene in a Chinese pedigree with retinitis pigmentosa and angle-closure glaucoma

2021 ◽  
Vol 21 (1) ◽  
Author(s):  
Wei-ning Li ◽  
Xiu-juan Du ◽  
Yu-ting Zhang ◽  
Le-yi Wang ◽  
Jing Zhu
Keyword(s):  
Visual Field ◽  
Retinitis Pigmentosa ◽  
Novel Mutation ◽  
Genetic Mutation ◽  
Angle Closure Glaucoma ◽  
Angle Closure ◽  
The Novel ◽  
Progressive Loss ◽  
Whole Exome ◽  
Transversion Mutation

Abstract Background Retinitis pigmentosa (RP) is a rare, progressive, and hereditary disorder that leads to the progressive loss of vision and visual field, and in some cases blindness. The specific relationship between RP and glaucoma has been debated for decades. Methods In this study, we examined a Han RP family with concomitant angle-closure glaucoma (ACG), performed an inductive analysis of their clinical features and assistant results, and applied whole-exome sequencing (WES) technology for a molecular diagnosis. Results A novel transversion mutation (c.626 T > A) was identified in the peripherin-2 (PRPH2) gene in the proband, resulting in the substitution of Valine to aspartic acid in codon 209. A full ophthalmic examination showed that the proband with the c.626 T > A mutation had a typical RP manifestation, with close angles; however, the proband’s elder brother, who lacked the novel mutation, had a normal fundus and open angles. Conclusion Our results extend the genetic mutation spectrum of PRPH2 in RP, and provide evidence to support a genetic correlation between RP and ACG.

A novel pathway for transversion mutation induced by dCTP misincorporation in a mutator strain of CHO cells

1989 ◽  
Vol 9 (4) ◽  
pp. 1810-1812
Author(s):  
G Phear ◽  
M Meuth
Keyword(s):  
Dna Replication ◽  
Cho Cells ◽  
Mutator Strain ◽  
Transversion Mutation

Intracellular imbalances of dCTP produce both T----C transitions and an unusual class of transversions (A----C) at the aprt locus of CHO cells. Our data suggest that this transversion pathway is the consequence of dCTP:T mispairs which are not efficiently proofread during DNA replication.

scholarly journals Human Cytomegalovirus Resistance to Deoxyribosylindole Nucleosides Maps to a Transversion Mutation in the Terminase Subunit-Encoding GeneUL89

2014 ◽  
Vol 59 (1) ◽  
pp. 226-232 ◽  
Author(s):  
Brian G. Gentry ◽  
Quang Phan ◽  
Ellie D. Hall ◽  
Julie M. Breitenbach ◽  
Katherine Z. Borysko ◽  
...  
Keyword(s):  
Human Cytomegalovirus ◽  
Structural Similarity ◽  
Open Reading Frames ◽  
Wild Type Virus ◽  
Wild Type ◽  
Term Administration ◽  
Transversion Mutation ◽  
Exon 1

ABSTRACTHuman cytomegalovirus (HCMV) infection can cause severe illnesses, including encephalopathy and mental retardation, in immunocompromised and immunologically immature patients. Current pharmacotherapies for treating systemic HCMV infections include ganciclovir, cidofovir, and foscarnet. However, long-term administration of these agents can result in serious adverse effects (myelosuppression and/or nephrotoxicity) and the development of viral strains with reduced susceptibility to drugs. The deoxyribosylindole (indole) nucleosides demonstrate a 20-fold greater activityin vitro(the drug concentration at which 50% of the number of plaques was reduced with the presence of drug compared to the number in the absence of drug [EC50] = 0.34 μM) than ganciclovir (EC50= 7.4 μM) without any observed increase in cytotoxicity. Based on structural similarity to the benzimidazole nucleosides, we hypothesize that the indole nucleosides target the HCMV terminase, an enzyme responsible for packaging viral DNA into capsids and cleaving the DNA into genome-length units. To test this hypothesis, an indole nucleoside-resistant HCMV strain was isolated, the open reading frames of the genes that encode the viral terminase were sequenced, and a G766C mutation in exon 1 ofUL89was identified; this mutation resulted in an E256Q change in the amino acid sequence of the corresponding protein. An HCMV wild-type strain, engineered with this mutation to confirm resistance, demonstrated an 18-fold decrease in susceptibility to the indole nucleosides (EC50= 3.1 ± 0.7 μM) compared to that of wild-type virus (EC50= 0.17 ± 0.04 μM). Interestingly, this mutation did not confer resistance to the benzimidazole nucleosides (EC50for wild-type HCMV = 0.25 ± 0.04 μM, EC50for HCMV pUL89 E256Q = 0.23 ± 0.04 μM). We conclude, therefore, that the G766C mutation that results in the E256Q substitution is unique for indole nucleoside resistance and distinct from previously discovered substitutions that confer both indole and benzimidazole nucleoside resistance (D344E and A355T).

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