Sequence analysis of spontaneously-arising mutations at the aprt locus in wild-type and thymidine kinase-deficient Friend cells: Evidence for strand slippage-misalignment mechanism in formation of deletions

1997 ◽  
Vol 25 (1) ◽  
pp. 127S-127S ◽  
Author(s):  
PAULA L. HYLAND ◽  
MARK W. MCKINNEY ◽  
ANNE L. KEEGAN ◽  
PATRICK. G. MCKENNA ◽  
MARTIN. D. CURRAN ◽  
...  
Keyword(s):  
Sequence Analysis ◽  
Thymidine Kinase ◽  
Wild Type ◽  
Friend Cells

Analysis of mutations at the adenine phosphoribosyltransferase gene locus in wild-type and thymidine kinase-deficient Friend cells

1996 ◽  
Vol 24 (1) ◽  
pp. 105S-105S ◽  
Author(s):  
Paula L. Hyland ◽  
Mark W. McKinney ◽  
Anne. L. Keegan ◽  
Patrick G. McKenna ◽  
Yvonne A. Barnett
Keyword(s):  
Thymidine Kinase ◽  
Gene Locus ◽  
Wild Type ◽  
Adenine Phosphoribosyltransferase ◽  
Friend Cells

scholarly journals The Identification of Mutation in BMP15 Gene Associated with Litter Size in Xinjiang Cele Black Sheep

Animals ◽  
2021 ◽  
Vol 11 (3) ◽  
pp. 668
Author(s):  
Zhi-gang Niu ◽  
Jin Qin ◽  
Yao Jiang ◽  
Xiang-Dong Ding ◽  
Yu-gong Ding ◽  
...  
Keyword(s):  
Sequence Analysis ◽  
Litter Size ◽  
Base Change ◽  
Wild Type ◽  
Wild Genotype ◽  
Exon 2 ◽  
Black Sheep ◽  
Morphogenetic Protein ◽  
Gene Sequence Analysis ◽  
Exon 1

The Bone Morphogenetic Protein 15 (BMP15) gene is known to have multiple single-nucleotide polymorphism sites associated with sheep fecundity. This study used gene sequence analysis and mutation detection assays for BMP15 by using 205 blood samples of ewes with known lambing records. Sequence analysis showed that mutation B1 missed the CTT base in exon 1 at positions 28–30, leading to a leucine deletion in the BMP15 protein. Litter size of ewes differed significantly between BB and B+ genotypes of B1 (p < 0.05); however, the differences between wild genotype (++) and homozygous (BB) or wild genotype (++) and heterozygous (B+) were not significant (p > 0.05). Another mutation, T755C, is a T-to-C base change at position 755 of exon 2, resulting in leucine replacement by proline at this position of the BMP15 protein (p.L252P). Two genotypes were identified in the flock: heterozygous (E+) and wild-type genotype (++). Ewes with heterozygous (E+) p.L252P had significantly larger litter sizes than those with the wild-type genotype (p < 0.05). Comprehensive analysis suggests that p.L252P is a mutation that affects fecundity in Cele black sheep.

scholarly journals The Valine Anticodon and Valylatability of Peanut Clump Virus RNAs Are Not Essential but Provide a Modest Competitive Advantage in Plants

2000 ◽  
Vol 74 (18) ◽  
pp. 8720-8725 ◽  
Author(s):  
Daiki Matsuda ◽  
Patrice Dunoyer ◽  
Odile Hemmer ◽  
Christiane Fritsch ◽  
Theo W. Dreher
Keyword(s):  
Sequence Analysis ◽  
Nicotiana Benthamiana ◽  
General Characteristic ◽  
Wild Type ◽  
Genomic Rnas ◽  
Viral Rnas ◽  
Fold Reduction ◽  
Direct Competition

ABSTRACT The role of valine aminoacylation of the two genomic RNAs ofPeanut clump virus (PCV) was studied by comparing the amplification in vivo of RNAs with GAC, GΔC, or CCA anticodons in the tRNA-like structure (TLS) present at the 3′ end of each viral RNA. The PCV RNA1 TLS of isolate PCV2 possesses a GAC anticodon and is capable of highly efficient valylation, whereas the RNA2 TLS has a GΔC anticodon that does not support valylation. The presence in RNA1 of GΔC or CCA anticodons that conferred nonvalylatability resulted in about 2- to 4-fold and a 14- to 24-fold reduction, respectively, in RNA accumulations in tobacco BY-2 protoplasts inoculated with the RNA1 variants together with wild-type RNA2(GΔC). No differences in RNA levels were observed among protoplasts inoculated with the three variant RNA2s in the presence of wild-type RNA1(GAC). All combinations of valylatable and nonvalylatable RNAs 1 and 2 were similarly infectious in Nicotiana benthamiana plants, and viral RNAs accumulated to similar levels; all input TLS sequences were present unchanged in apical leaves. In direct competition experiments in N. benthamiana plants, however, both RNA1 and RNA2 with GAC valylatable anticodons outcompeted the nonvalylatable variants. We conclude that valylation provides a small but significant replicational advantage to both PCV RNAs. Sequence analysis of the TLS from RNA2 of a second PCV isolate, PO2A, revealed the presence of an intact GAC valine anticodon, suggesting that the differential valylation of the genomic RNAs of isolate PCV2 is not a general characteristic of PCV.

Mutations in the yeast RNA14 and RNA15 genes result in an abnormal mRNA decay rate; sequence analysis reveals an RNA-binding domain in the RNA15 protein

1991 ◽  
Vol 11 (6) ◽  
pp. 3075-3087
Author(s):  
L Minvielle-Sebastia ◽  
B Winsor ◽  
N Bonneaud ◽  
F Lacroute
Keyword(s):  
Molecular Weight ◽  
Sequence Analysis ◽  
Decay Rate ◽  
Rna Binding ◽  
Binding Domain ◽  
Temperature Sensitive ◽  
Multicopy Plasmid ◽  
Wild Type ◽  
Rna Binding Domain ◽  
Temperature Sensitive Phenotype

In Saccharomyces cerevisiae, temperature-sensitive mutations in the genes RNA14 and RNA15 correlate with a reduction of mRNA stability and poly(A) tail length. Although mRNA transcription is not abolished in these mutants, the transcripts are rapidly deadenylated as in a strain carrying an RNA polymerase B(II) temperature-sensitive mutation. This suggests that the primary defect could be in the control of the poly(A) status of the mRNAs and that the fast decay rate may be due to the loss of this control. By complementation of their temperature-sensitive phenotype, we have cloned the wild-type genes. They are essential for cell viability and are unique in the haploid genome. The RNA14 gene, located on chromosome H, is transcribed as three mRNAs, one major and two minor, which are 2.2, 1.5, and 1.1 kb in length. The RNA15 gene gives rise to a single 1.2-kb transcript and maps to chromosome XVI. Sequence analysis indicates that RNA14 encodes a 636-amino-acid protein with a calculated molecular weight of 75,295. No homology was found between RNA14 and RNA15 or between RNA14 and other proteins contained in data banks. The RNA15 DNA sequence predicts a protein of 296 amino acids with a molecular weight of 32,770. Sequence comparison reveals an N-terminal putative RNA-binding domain in the RNA15-encoded protein, followed by a glutamine and asparagine stretch similar to the opa sequences. Both RNA14 and RNA15 wild-type genes, when cloned on a multicopy plasmid, are able to suppress the temperature-sensitive phenotype of strains bearing either the rna14 or the rna15 mutation, suggesting that the encoded proteins could interact with each other.

A Herbicide Resistant Euglena Mutant Carrying a Ser to Thr Substitution at Position 265 in the D1 Protein of Photosystem II

1992 ◽  
Vol 47 (3-4) ◽  
pp. 245-248 ◽  
Author(s):  
A. Aiach ◽  
E. Ohmann ◽  
U. Bodner ◽  
U. Johanningmeier
Keyword(s):  
Amino Acids ◽  
Sequence Analysis ◽  
Photosystem Ii ◽  
D1 Protein ◽  
Inhibitory Effect ◽  
Wild Type ◽  
Rna Sequence ◽  
Herbicide Resistant ◽  
Lower Resistance ◽  
Chlamydomonas Mutants

A herbicide resistant Euglena mutant (MSI) has been obtained by adapting wild type cells to increasing concentrations of DCMU (3-(3′,4′-dichlorophenyl)-1,1-dimethylurea). Lower resistance levels towards DCMU and metribuzin were observed in MSI when compared with Euglena or Chlamydomonas mutants with Ser 264 to Ala substitutions. RNA-sequence analysis identified a Ser to Thr change at position 265 (equivalent to position 264 in other organisms), thus making it possible to compare the influence of amino acids Ser, Ala and Thr at identical positions on the inhibitory effect of structurally different herbicides in the same species.

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