Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/46166
標題: Sequence diversity of beta-tubulin (tubA) gene in Phaeosphaeria nodorum and P. avenaria
作者: Malkus, A.
張碧芳
Reszka, E.
Chang, C.J.
Arseniuk, E.
Chang, P.F.L.
Ueng, P.P.
關鍵字: beta w-tubulin;Phaeosphaeria;wheat;small-grain cereals;stagonospora-nodorum;benomyl-resistance;septoria;diseases;selectable marker;wheat;barley;differentiation;identification;expression
Project: Fems Microbiology Letters
期刊/報告no:: Fems Microbiology Letters, Volume 249, Issue 1, Page(s) 49-56.
摘要: 
Full-length coding sequences of the beta-tubulin gene (tubA) were PCR-amplified and sequenced from 42 Phaeosphaeria isolates, including, 16 P. nodorum and 23 P. avenaria species from cereals, two Polish isolates from rye (Secale cereale L.), and one isolate from dallis grass (Paspalum dilatatum Poir). A tubA gene of size 1556 bp was identified in wheat- and barley-biotype P. nodorum (PN-w and PN-b), P. avenaria f. sp. avenaria (Paa), homothallic P. avenaria f. sp. triticea (P.a.t.) (Pat1) and the P.a.t. isolate (Pat3) from the State of Washington. The tubA gene length polymorphisms were detected in two P.a.t. isolates (Pat2) from foxtail barley (Hordeum jubatum L.), one from dallis grass and two Polish isolates from rye. These size differences were due to the variation of intron lengths among these three Phaeosphaeria species. All Phaeosphaeria isolates have identical 1344 bp exons that can be translated into a 447 amino acid P-tubulin. Like glyceraldehyde-3-phosphate dehydrogenase, the P-tubulin amino acid sequence was identical in all Phaeosphaeria species used in this study, with the exception of the two Pat2 isolates. Six amino acid differences were evident in the P-tubulin of these Pat2 isolates. (c) 2005 Federation of European Microbiological Societies. Published by Elsevier B.V. All rights reserved.
URI: http://hdl.handle.net/11455/46166
ISSN: 0378-1097
DOI: 10.1016/j.femsle.2005.05.049
Appears in Collections:植物病理學系

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