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3 results on '"Mertz, Rachel A."'

1. The Cell Wall Arabinose-Deficient Arabidopsis thaliana Mutant murus5 Encodes a Defective Allele of REVERSIBLY GLYCOSYLATED POLYPEPTIDE2.

Author

Dugard CK, Mertz RA, Rayon C, Mercadante D, Hart C, Benatti MR, Olek AT, SanMiguel PJ, Cooper BR, Reiter WD, McCann MC, and Carpita NC

Subjects
Alleles, Arabidopsis genetics, Arabidopsis Proteins chemistry, Arabinose genetics, Cell Wall genetics, Chromosome Mapping, Chromosomes, Plant, Gene Expression Regulation, Plant, Genetic Complementation Test, Glucosyltransferases chemistry, High-Throughput Nucleotide Sequencing, Mutation, Plants, Genetically Modified, Protein Domains, Protein Folding, Protein Stability, Sequence Homology, Amino Acid, Arabidopsis cytology, Arabidopsis Proteins genetics, Arabidopsis Proteins metabolism, Arabinose metabolism, Cell Wall metabolism, Glucosyltransferases genetics, Glucosyltransferases metabolism
Abstract

Traditional marker-based mapping and next-generation sequencing was used to determine that the Arabidopsis (Arabidopsis thaliana) low cell wall arabinose mutant murus5 (mur5) encodes a defective allele of REVERSIBLY GLYCOSYLATED POLYPEPTIDE2 (RGP2). Marker analysis of 13 F2 confirmed mutant progeny from a recombinant mapping population gave a rough map position on the upper arm of chromosome 5, and deep sequencing of DNA from these 13 lines gave five candidate genes with G→A (C→T) transitions predicted to result in amino acid changes. Of these five, only insertional mutant alleles of RGP2, a gene that encodes a UDP-arabinose mutase that interconverts UDP-arabinopyranose and UDP-arabinofuranose, exhibited the low cell wall arabinose phenotype. The identities of mur5 and two SALK insertional alleles were confirmed by allelism tests and overexpression of wild-type RGP2 complementary DNA placed under the control of the 35S promoter in the three alleles. The mur5 mutation results in the conversion of cysteine-257 to tyrosine-257 within a conserved hydrophobic cluster predicted to be distal to the active site and essential for protein stability and possible heterodimerization with other isoforms of RGP., (© 2016 American Society of Plant Biologists. All Rights Reserved.)

Published
2016
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2. Alterations in cell-wall glycosyl linkage structure of Arabidopsis murus mutants.

Author

Mertz RA, Olek AT, and Carpita NC

Subjects
Genes, Plant, Glycosylation, Mutation, Principal Component Analysis, Arabidopsis genetics, Cell Wall chemistry, Monosaccharides analysis, Polysaccharides analysis
Abstract

Methylation (glycosyl-linkage) analyses of the cell walls from Arabidopsis (Arabidopsis thaliana L., Heynh.) murus mutants revealed variations in the linkage structure compared to wild type. Linkage analyses revealed new features for mutations whose defective gene has not been identified. For example, the low-rhamnose mur8 mutant also shows deficiencies in 4-GalA linkages. No change in the 2-Rha to 2,4-Rha ratio indicates the mutant had lower amounts of rhamnogalacturonan I, but no alteration in its fine structure. For all mur mutants, methylation analysis revealed that changes in other polysaccharides occur indirectly as a result of mutation. All mutants were resolved by Principal Components Analyses applied to normalized mole% values for the total set of linkage groups. The 'loadings' responsible for discrimination of mutant and wild type revealed variation in linkage groups otherwise difficult to discern and, in certain instances when the gene is known, resolved the specific deficiency from indirect effects altering other sugar linkage distributions., (Copyright © 2012 Elsevier Ltd. All rights reserved.)

Published
2012
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3. The Cell Wall Arabinose-Deficient Arabidopsis thaliana Mutant murus5 Encodes a Defective Allele of REVERSIBLY GLYCOSYLATED POLYPEPTIDE21[OPEN]

Author

Dugard, Christopher K., Mertz, Rachel A., Rayon, Catherine, Mercadante, Davide, Hart, Christopher, Benatti, Matheus R., Olek, Anna T., SanMiguel, Phillip J., Cooper, Bruce R., Reiter, Wolf-Dieter, McCann, Maureen C., and Carpita, Nicholas C.

Subjects
Protein Folding, Sequence Homology, Amino Acid, Arabidopsis Proteins, Protein Stability, Genetic Complementation Test, Arabidopsis, food and beverages, Chromosome Mapping, High-Throughput Nucleotide Sequencing, Articles, biochemical phenomena, metabolism, and nutrition, Plants, Genetically Modified, Arabinose, Chromosomes, Plant, carbohydrates (lipids), Protein Domains, Cell Wall, Gene Expression Regulation, Plant, Glucosyltransferases, Mutation, Alleles
Abstract

Traditional marker-based mapping and next-generation sequencing was used to determine that the Arabidopsis (Arabidopsis thaliana) low cell wall arabinose mutant murus5 (mur5) encodes a defective allele of REVERSIBLY GLYCOSYLATED POLYPEPTIDE2 (RGP2). Marker analysis of 13 F2 confirmed mutant progeny from a recombinant mapping population gave a rough map position on the upper arm of chromosome 5, and deep sequencing of DNA from these 13 lines gave five candidate genes with G→A (C→T) transitions predicted to result in amino acid changes. Of these five, only insertional mutant alleles of RGP2, a gene that encodes a UDP-arabinose mutase that interconverts UDP-arabinopyranose and UDP-arabinofuranose, exhibited the low cell wall arabinose phenotype. The identities of mur5 and two SALK insertional alleles were confirmed by allelism tests and overexpression of wild-type RGP2 complementary DNA placed under the control of the 35S promoter in the three alleles. The mur5 mutation results in the conversion of cysteine-257 to tyrosine-257 within a conserved hydrophobic cluster predicted to be distal to the active site and essential for protein stability and possible heterodimerization with other isoforms of RGP.

Published
2016

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