A single point mutation of hamster aminoacyl‐tRNA synthetase causes apoptosis by deprivation of cognate amino acid residue

The DNA sequence of a 196 base pair (bp) region of the acetolactate synthase (ALS) genes of three weed species, kochia, prickly lettuce, and Russian thistle, was determined. This region encompasses the coding sequence for Domain A, a region of the amino acid sequence previously demonstrated to play a pivotal role in conferring resistance to herbicides that inhibit ALS. The Domain A DNA sequence from a chlorsulfuron-resistant (R) prickly lettuce biotype from Idaho differed from that of a chlorsulfuron-susceptible (S) biotype by a single point mutation, which substituted a histidine for a proline. The Domain A DNA sequence from an R kochia biotype from Kansas also differed from that of an S biotype by a single point mutation in the same proline codon. This point mutation, however, conferred substitution of threonine for proline. Two different ALS-homologous sequences were isolated from an R biotype of Russian thistle. Neither sequence encoded amino acid substitutions in Domain A that differed from the consensus S sequence. The DNA sequence variation among the R and S kochia biotypes was used to characterize six Ada County, Idaho, kochia collections for correlation between phenotypic chlorsulfuron susceptibility and restriction digest patterns (RFLPs) of polymerase chain reaction amplification products. Most collections showed excellent correspondence between the RFLP patterns and the phenotypic response to chlorsulfuron application. However, one entirely R collection had the RFLP pattern of the S biotype, suggesting that resistance was not due to mutation in the proline codon.

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Point mutation in acetolactate synthase confers sulfonylurea and imidazolinone herbicide resistance in spiny annual sow-thistle [Sonchus asper (L.) Hill]

Canadian Journal of Plant Science ◽

10.4141/cjps2011-159 ◽

2012 ◽

Vol 92 (2) ◽

pp. 303-309 ◽

Cited By ~ 6

Author(s):

Kee Woong Park ◽

Judith M. Kolkman ◽

Carol A. Mallory-Smith

Keyword(s):

Amino Acid ◽

Point Mutation ◽

Herbicide Resistance ◽

Single Point ◽

Acetolactate Synthase ◽

Amino Acid Sequences ◽

Cross Resistance ◽

Single Point Mutation ◽

Sonchus Asper

Park, K. W., Kolkman, J. M. and Mallory-Smith, C. A. 2012. Point mutation in acetolactate synthase confers sulfonylurea and imidazolinone herbicide resistance in spiny annual sow-thistle [Sonchus asper (L.) Hill]. Can. J. Plant Sci. 92: 303–309. Suspected thifensulfuron resistant spiny annual sow-thistle was identified near Colfax, Washington, in two fields with a winter wheat and lentil rotation. Therefore, studies were conducted to examine resistance of spiny annual sow-thistle to thifensulfuron and cross-resistance to other acetolactate synthase inhibitors and to determine the physiological and molecular basis for herbicide resistance. Whole-plant bioassay confirmed that the biotype was highly resistant to the sulfonylurea (SU) herbicides, thifensulfuron, metsulfuron, and prosulfuron. The resistant (R) biotype was also highly resistant to the imidazolinone (IMI) herbicides, imazamox and imazethapyr. An in vivo acetolactate synthase (ALS) assay indicated that the concentrations of SU and IMI herbicides required for 50% inhibition (I50) were more than 10 times greater for R biotype compared with susceptible (S) biotype. Analysis of the nucleotide and predicted amino acid sequences for ALS genes demonstrated a single-point mutation from C to T at the als1 gene, conferring the substitution of the amino acid leucine for proline in the R biotype at position197. The results of this research indicate that the resistance of spiny annual sow-thistle to SU and IMI herbicides is due to on altered target site and caused by a point mutation in the als1 gene.

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A hamster temperature‐sensitive G1 mutant, tsBN250 has a single point mutation in histidyl‐tRNA synthetase that inhibits an accumulation of cyclin D1

Genes to Cells ◽

10.1046/j.1365-2443.1996.d01-227.x ◽

1996 ◽

Vol 1 (12) ◽

pp. 1101-1112 ◽

Cited By ~ 13

Author(s):

Seiichi Motomura ◽

Kohtaro Fukushima ◽

Hideo Nishitani ◽

Hajime Nawata ◽

Takeharu Nishimoto

Keyword(s):

Cyclin D1 ◽

Point Mutation ◽

Single Point ◽

Trna Synthetase ◽

Single Point Mutation ◽

Temperature Sensitive

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Site-specific single point mutation by anthranilic acid in hIAPP8–37 enhances anti-amyloidogenic activity

RSC Chemical Biology ◽

10.1039/d0cb00178c ◽

2021 ◽

Vol 2 (1) ◽

pp. 266-273

Author(s):

Sourav Kalita ◽

Sujan Kalita ◽

Ashim Paul ◽

Manisha Shah ◽

Sachin Kumar ◽

...

Keyword(s):

Amino Acid ◽

Point Mutation ◽

Anthranilic Acid ◽

Single Point ◽

Single Point Mutation ◽

Amyloid Formation ◽

Site Specific

β-Amino acid based peptidomimetics are attractive scaffolds for therapeutics design towards T2D. They prevent amyloid formation of hIAPP by forming non-fibrillar non-toxic aggregates.

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Faculty Opinions recommendation of Unraveling adaptive evolution: how a single point mutation affects the protein coregulation network.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1041005.489903 ◽

2006 ◽

Author(s):

Mark D Adams

Keyword(s):

Point Mutation ◽

Adaptive Evolution ◽

Single Point ◽

Single Point Mutation

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Faculty Opinions recommendation of One small step for a yeast--microevolution within macrophages renders Candida glabrata hypervirulent due to a single point mutation.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.724428301.793504585 ◽

2015 ◽

Author(s):

Joseph Heitman ◽

Blake Billmyre

Keyword(s):

Point Mutation ◽

Candida Glabrata ◽

Single Point ◽

Single Point Mutation ◽

Small Step

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Dominant-negative inhibition of pheromone receptor signaling by a single point mutation in the G protein α subunit. Vol. 279 (2004) 35287-35297

Journal of Biological Chemistry ◽

10.1016/s0021-9258(20)56430-2 ◽

2005 ◽

Vol 280 (33) ◽

pp. 29988

Author(s):

Yuh-Lin Wu ◽

Shelley B. Hooks ◽

T. Kendall Harden ◽

Henrik G. Dohlman

Keyword(s):

G Protein ◽

Point Mutation ◽

Single Point ◽

Dominant Negative ◽

Single Point Mutation ◽

Receptor Signaling ◽

Α Subunit ◽

Pheromone Receptor ◽

G Protein Α Subunit

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A Single Point Mutation, Asn16→Lys, Dictates the Temperature-Sensitivity of the Reovirus tsG453 Mutant

Viruses ◽

10.3390/v13020289 ◽

2021 ◽

Vol 13 (2) ◽

pp. 289

Author(s):

Kathleen K. M. Glover ◽

Danica M. Sutherland ◽

Terence S. Dermody ◽

Kevin M. Coombs

Keyword(s):

Amino Acid ◽

Temperature Sensitivity ◽

Reverse Genetics ◽

Core Protein ◽

Single Point ◽

Single Amino Acid ◽

Single Point Mutation ◽

Temperature Sensitive ◽

Amino Acid Substitutions ◽

Gene Encoding

Studies of conditionally lethal mutants can help delineate the structure-function relationships of biomolecules. Temperature-sensitive (ts) mammalian reovirus (MRV) mutants were isolated and characterized many years ago. Two of the most well-defined MRV ts mutants are tsC447, which contains mutations in the S2 gene encoding viral core protein σ2, and tsG453, which contains mutations in the S4 gene encoding major outer-capsid protein σ3. Because many MRV ts mutants, including both tsC447 and tsG453, encode multiple amino acid substitutions, the specific amino acid substitutions responsible for the ts phenotype are unknown. We used reverse genetics to recover recombinant reoviruses containing the single amino acid polymorphisms present in ts mutants tsC447 and tsG453 and assessed the recombinant viruses for temperature-sensitivity by efficiency-of-plating assays. Of the three amino acid substitutions in the tsG453 S4 gene, Asn16-Lys was solely responsible for the tsG453ts phenotype. Additionally, the mutant tsC447 Ala188-Val mutation did not induce a temperature-sensitive phenotype. This study is the first to employ reverse genetics to identify the dominant amino acid substitutions responsible for the tsC447 and tsG453 mutations and relate these substitutions to respective phenotypes. Further studies of other MRV ts mutants are warranted to define the sequence polymorphisms responsible for temperature sensitivity.

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A single point mutation converts a proton-pumping rhodopsin into a red-shifted, turn-on fluorescent sensor for chloride

Chemical Science ◽

10.1039/d0sc06061e ◽

2021 ◽

Author(s):

Jasmine N. Tutol ◽

Jessica Lee ◽

Hsichuan Chi ◽

Farah N. Faizuddin ◽

Sameera S. Abeyrathna ◽

...

Keyword(s):

Point Mutation ◽

Fluorescent Sensor ◽

Single Point ◽

Proton Pumping ◽

Single Point Mutation ◽

Turn On ◽

Gloeobacter Violaceus

By utilizing laboratory-guided evolution, we have converted the fluorescent proton-pumping rhodopsin GR from Gloeobacter violaceus into GR1, a red-shifted, turn-on fluorescent sensor for chloride.

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