Infection with the Obligate Biotroph Plasmodiophora braßicae, the Causal Agent of the Club Root Disease, does not Affect Expreßion of NIT-1/2-related Nitrilases in Roots of Chinese Cabbage

Bischoff, Markus; Löw, Rainer; Grsic, Slobodanka; Rausch, Thomas; Hilgenberg, Willy; Ludwig‐Müller, Jutta

doi:10.1016/s0176-1617(11)82164-4

Cited by 21 publications

(32 citation statements)

References 18 publications

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“…Moreover, suppression of NIT1 and NIT2 expression with an antisense RNA strategy has been reported to delay clubroot development in Arabidopsis plants, suggesting that the IAN pathway plays an important role in IAA synthesis for clubroot formation (Neuhaus et al 2000). In Chinese cabbage, the increase of nitrilase transcripts is not evident during clubroot development, although nitrilase activity is enhanced (Bischoff et al 1995;Grsic et al 1999). Recently, transcription of one of the three nitrilase genes (BrNIT-T1) following P. brassicae infection was reported in turnips (Ishikawa et al 2007).…”

Section: Introductionmentioning

confidence: 55%

“…A neighbor-joining phylogenetic tree was constructed with deduced NIT amino acid sequences. Full-length sequences of amino acids were used, except for BrNIT3, which lacked an N-terminal sequence, along with partial sequences of BcNIT1, BcNIT2, and BcNIT4, which were reported previously (Grsic et al 1999 (Bischoff et al 1995;Grsic et al 1999), although BrNIT3 fell within the cluster. BrNIT-T4 (BrNIT4) was included in the NIT4 cluster, and was most similar to BcNIT4.…”

Section: Resultsmentioning

confidence: 99%

“…The parameters for PCR were 40 cycles at 94°C for 30 s, 49°C for 1 min, and 72°C for 1 min. Partial cDNA was amplified using the perfect match primer for NIT1 of A. thaliana (Bischoff et al 1995;Supplemental Table S1). …”

Section: Isolation Of Nit From Chinese Cabbagementioning

confidence: 99%

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Alternative transcription initiation of the nitrilase gene (BrNIT2) caused by infection with Plasmodiophora brassicae Woron. in Chinese cabbage (Brassica rapa L.)

et al. 2008

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In clubroot disease, gall formation is induced by infection with the obligate biotroph Plasmodiophora brassicae, and cell hypertrophy is dependent on increased auxin levels. The enzyme nitrilase is suggested to play an important role in auxin biosynthesis in plants. Here, we investigated the expression of nitrilase genes in clubroot disease in Chinese cabbage (Brassica rapa L.). We isolated four isogenes of nitrilase (BrNIT1, BrNIT2, BrNIT3, and BrNIT4) from Chinese cabbage. When a BrNIT2-specific probe was used for Northern blot hybridization, enhanced accumulation of a 1.4 kb mRNA and additional shorter transcripts (1.1 kb) were only detected in clubbed roots 25 days postinoculation (dpi) onward. The expression of BrNIT1 was not strongly affected by infection with P. brassicae. BrNIT3 expression was detected in the roots at 10 and 20 dpi, and the expression was less in clubbed roots than in healthy roots at 20 dpi. Analysis of the transcription initiation point of the BrNIT2 gene suggests that 1.1 kb transcripts were generated by alternative transcription initiation between the second intron and the third exon. The sequence from the second intron to half of the third exon (+415 to +1037, 623 bp) had promoter activity in Arabidopsis during clubroot formation. Therefore, our results suggest that transcriptional regulation of BrNIT2 might be involved in auxin overproduction during clubroot development.

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Section: Introductionmentioning

confidence: 55%

Section: Resultsmentioning

confidence: 99%

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Alternative transcription initiation of the nitrilase gene (BrNIT2) caused by infection with Plasmodiophora brassicae Woron. in Chinese cabbage (Brassica rapa L.)

et al. 2008

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“…Genomic or cDNA sequences of nitrilases are now known from A. thaliana, two Brassica species (B. campestris and Brassica oleracea) (15,16), tobacco (N. tabacum) (17), and rice (O. sativa, GenBank TM accession number AB027054). In addition several expressed sequence tag clones exist, which encode nitrilase-like proteins.…”

Section: Discussionmentioning

confidence: 99%

“…Are not Restricted to BrassicaceaePartial or complete cDNA or genomic sequences of nitrilases are known from several plant species like A. thaliana (1-3), Brassica campestris (Chinese cabbage) (15,16), Lotus japonicus (GenBank TM accession number AW720658), N. tabacum (tobacco) (8), and Oryza sativa (rice) (GenBank TM accession number AB027054). By comparing the homologies between these nitrilases ( Fig.…”

Section: Nitrilase 4 Isoformsmentioning

confidence: 95%

The Arabidopsis thaliana Isogene NIT4 and Its Orthologs in Tobacco Encode β-Cyano-l-alanine Hydratase/Nitrilase

Piotrowski

Schönfelder

Weiler

2001

Journal of Biological Chemistry

180

182

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Nitrilases (nitrile aminohydrolases, EC 3.5.5.1) are enzymes that catalyze the hydrolysis of nitriles to the corresponding carbon acids. Among the four known nitrilases of Arabidopsis thaliana, the isoform NIT4 is the most divergent one, and homologs of NIT4 are also known from species not belonging to the Brassicaceae like Nicotiana tabacum and Oryza sativa. We expressed A. thaliana NIT4 as hexahistidine tag fusion protein in Escherichia coli. The purified enzyme showed a strong substrate specificity for ␤-cyano-L-alanine (Ala(CN)), an intermediate product of cyanide detoxification in higher plants. Interestingly, not only aspartic acid but also asparagine were identified as products of NIT4-catalyzed Ala(CN) hydrolysis. Asn itself was no substrate for NIT4, indicating that it is not an intermediate but one of two reaction products. NIT4 therefore has both nitrilase and nitrile hydratase activity. Several lines of evidence indicate that the catalytic center for both reactions is the same. The NIT4 homologs of N. tabacum were found to catalyze the same reactions and protein extracts of A. thaliana, N. tabacum and Lupinus angustifolius also converted Ala(CN) to Asp and Asn in vitro. NIT4 may play a role in cyanide detoxification during ethylene biosynthesis because extracts from senescent leaves of A. thaliana showed higher Ala(CN) hydratase/nitrilase activities than extracts from nonsenescent tissue.

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Control of clubroot of crucifers byPhoma glomerataand its product epoxydon

et al. 1999

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library and identi®ed another cytochrome P450 cDNA from C quinquefasciatus larvae.The PCR products of c250 bp were ampli®ed, and 35 and 29 clones from permethrin-suseceptible and -resistant JPal-per strains, respectively, were sequenced. Alignments of the deduced amino acid sequences from these clones revealed that there were seven distinct sequences. One of these clones, which accounted for more than 57% of the total clones, was used as a probe to re-screen the cDNA library. Another full-length cDNA was cloned and designated CYP6F1. Northern blot analysis revealed that the CYP6F1 gene in JPal-per strain appeared to be expressed more strongly than that in the S strain suggesting a possible involvement of this gene in resistance to pyrethroids. This result supports our previous ®nding that the content of cytochrome P450 was about 2.7 times higher in JPal-per strain than in the S strain. 1 Results of Southern blotting indicated that CYP6F1 genes from susceptible and JPal-per strains contain different Eco RI and Eco RV digestion sites, suggesting that these two strains have different genome structures.

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Infection with the Obligate Biotroph Plasmodiophora braßicae, the Causal Agent of the Club Root Disease, does not Affect Expreßion of NIT-1/2-related Nitrilases in Roots of Chinese Cabbage

Cited by 21 publications

References 18 publications

Alternative transcription initiation of the nitrilase gene (BrNIT2) caused by infection with Plasmodiophora brassicae Woron. in Chinese cabbage (Brassica rapa L.)

Alternative transcription initiation of the nitrilase gene (BrNIT2) caused by infection with Plasmodiophora brassicae Woron. in Chinese cabbage (Brassica rapa L.)

The Arabidopsis thaliana Isogene NIT4 and Its Orthologs in Tobacco Encode β-Cyano-l-alanine Hydratase/Nitrilase

Control of clubroot of crucifers byPhoma glomerataand its product epoxydon

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