Construction and characterization of the IGF Arabidopsis BAC library

Mozo, Teresa; Fischer, Sabine; Shizuya, Hiroaki; Altmann, Thomas

doi:10.1007/s004380050769

Cited by 91 publications

(34 citation statements)

References 41 publications

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“…Before the sequencing in this region of chromosome V was complete, a candidate SCPL gene ( T22D6.200 ) was identified on two overlapping bacterial artificial chromosomes (BACs), F24L14 and F27P17 (Figure 4), by probing a BAC library of Col‐0 genomic DNA (Mozo et al ., 1998) with cDNA from eight SCPL ESTs with no known genomic position. Sequencing of this gene from the sng2 mutant did not reveal an EMS‐induced mutation, and transformation of sng2 plants with a binary vector carrying the wild‐type allele did not result in complementation of the mutant phenotype (data not shown).…”

Section: Resultsmentioning

confidence: 99%

The sng2 mutant of Arabidopsis is defective in the gene encoding the serine carboxypeptidase‐like protein sinapoylglucose:choline sinapoyltransferase

Shirley

McMichael

Chapple³

2001

The Plant Journal

104

136

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SummarySerine carboxypeptidase-like (SCPL) proteins have traditionally been assigned roles in the hydrolytic processing of proteins; however, several SCPL proteins have recently been identi®ed as catalysts in transacylation reactions of plant secondary metabolism. The novel functions of these enzymes suggest a catalytic diversity for plant SCPL proteins that extends beyond simple hydrolysis reactions. Characterization of the Arabidopsis sng2 (sinapoylglucose accumulator 2) mutant has identi®ed another SCPL protein involved in plant secondary metabolism. The sng2 mutant was isolated by screening seed extracts for altered levels of sinapate esters, a group of phenylpropanoid compounds found in Arabidopsis and some other members of the Brassicaceae. Homozygous sng2 seeds accumulate sinapoylglucose instead of sinapoylcholine, and have increased levels of choline and decreased activity of the enzyme sinapoylglucose:choline sinapoyltransferase (SCT). Cloning of the SNG2 gene by a combination of map-based and candidate gene approaches demonstrates that SCT is another member of the growing class of SCPL acyltransferases involved in plant secondary metabolism.

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Section: Resultsmentioning

confidence: 99%

The sng2 mutant of Arabidopsis is defective in the gene encoding the serine carboxypeptidase‐like protein sinapoylglucose:choline sinapoyltransferase

Shirley

McMichael

Chapple³

2001

The Plant Journal

104

136

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“…1999 ). Clones from a bacterial artificial chromosome (BAC) library of Col‐0 genomic DNA ( Mozo et al . 1998 ) were obtained using p3037‐3 as a hybridization probe.…”

Section: Resultsmentioning

confidence: 99%

“…Filters containing clones from a bacterial artificial chromosome (BAC) library of Col‐0 DNA (IGF BAC library, Mozo et al . 1998 ) were provided by RZPD (Berlin, Germany), and individual BAC clones identified by hybridization to radiolabelled p3037‐3 DNA.…”

Section: Methodsmentioning

confidence: 99%

RPP13 is a simple locus in Arabidopsis thaliana for alleles that specify downy mildew resistance to different avirulence determinants in Peronospora parasitica

Bittner-Eddy¹,

Crute

Holub³

et al. 2000

The Plant Journal

255

154

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SummaryDisease resistance (R) genes are found in plants as either simple (single allelic series) loci, or more frequently as complex loci of tandemly repeated genes. These different loci are likely to be under similar evolutionary forces from pathogens, but the contrast between them suggests important differences in mechanisms associated with DNA structure and recombination that generate and maintain R gene diversity. The RPP13 locus in Arabidopsis represents an important paradigm for studying the evolution of an R gene at a simple locus. The RPP13 allele from the accession Nd-1, designated RPP13-Nd, confers resistance to ®ve different isolates of the biotrophic oomycete, Peronospora parasitica (causal agent of downy mildew), and encodes an NBS-LRR type R protein with a putative amino-terminal leucine zipper. The RPP13-Rld allele, cloned from the accession Rld-2, encodes a different speci®city. Comparison of three RPP13 alleles revealed a high rate of amino acid divergence within the LRR domain, less than 80% identity overall, compared to the remainder of the protein (>95% identity). We also found evidence for positive selection in the LRR domain for amino acid diversi®cation outside the core conserved b-strand/ b-turn motif, suggesting that more of the LRR structure is available for interaction with target molecules than has previously been reported for other R gene products. Furthermore, an amino acid sequence (LLRVLDL) identical in an LRR among RPP13 alleles is conserved in other LZ NBS-LRR type R proteins, suggesting functional signi®cance.

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“…YAC clones were obtained from the Arabidopsis Biological Resource Center (ABRC) at Ohio State University, and the BAC clone F24J7 was obtained from RZPD (Berlin, Germany; Mozo et al. , 1998).…”

Section: Methodsmentioning

confidence: 99%

Two TIR:NB:LRR genes are required to specify resistance to Peronospora parasitica isolate Cala2 in Arabidopsis

Williams²,

et al. 2004

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These authors made an equal contribution to the work reported. SummaryResistance responses that plants deploy in defence against pathogens are often triggered following a recognition event mediated by resistance (R) genes. The encoded R proteins usually contain a nucleotide-binding site (NB) and a leucine-rich repeat (LRR) domain. They are further classi®ed into those that contain an N-terminal coiled coil (CC) motif or a Toll interleukin receptor (TIR) domain. Such R genes, when transferred into a susceptible plant of the same or closely related species, usually impart full resistance capability. We have used map-based cloning and mutation analysis to study the recognition of Peronospora parasitica (RPP)2 (At) locus in Arabidopsis accession Columbia (Col-0), which is a determinant of speci®c recognition of P. parasitica (At) isolate Cala2. Genetic mapping located RPP2 to a 200-kb interval on chromosome 4, which contained four adjacent TIR:NB:LRR genes. Mutational analysis revealed three classes of genes involved in specifying resistance to Cala2. One class, which resulted in pleiotropic effects on resistance to other P. parasitica (At) isolates, was unlinked to the RPP2 locus; this class included AtSGT1b. The other two classes were mapped within the interval and were speci®c to Cala2 resistance. Representatives of each of these classes were sequenced, and mutations were found in one or the other of two (RPP2A and RPP2B) of the four TIR:NB:LRR genes. RPP2A and RPP2B complemented their speci®c mutations, but failed to impart resistance when present alone, and it is concluded that both genes are essential determinants for isolate-speci®c recognition of Cala2. RPP2A has an unusual structure with a short LRR domain at the Cterminus, preceded by two potential but incomplete TIR:NB domains. In addition, the RPP2A LRR domain lacks conserved motifs found in all but three other TIR:NB:LRR class proteins. In contrast, RPP2B has a complete TIR:NB:LRR structure. It is concluded that RPP2A and RPP2B cooperate to specify Cala2 resistance by providing recognition or signalling functions lacked by either partner protein.

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Construction and characterization of the IGF Arabidopsis BAC library

Cited by 91 publications

References 41 publications

The sng2 mutant of Arabidopsis is defective in the gene encoding the serine carboxypeptidase‐like protein sinapoylglucose:choline sinapoyltransferase

The sng2 mutant of Arabidopsis is defective in the gene encoding the serine carboxypeptidase‐like protein sinapoylglucose:choline sinapoyltransferase

RPP13 is a simple locus in Arabidopsis thaliana for alleles that specify downy mildew resistance to different avirulence determinants in Peronospora parasitica

Two TIR:NB:LRR genes are required to specify resistance to Peronospora parasitica isolate Cala2 in Arabidopsis

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