Transcript and proteomic analysis of developing white lupin (Lupinus albus L.) roots

Abstract

BackgroundWhite lupin (Lupinus albus L.) roots efficiently take up and accumulate (heavy) metals, adapt to phosphate deficiency by forming cluster roots, and secrete antimicrobial prenylated isoflavones during development. Genomic and proteomic approaches were applied to identify candidate genes and proteins involved in antimicrobial defense and (heavy) metal uptake and translocation.ResultsA cDNA library was constructed from roots of white lupin seedlings. Eight thousand clones were randomly sequenced and assembled into 2,455 unigenes, which were annotated based on homologous matches in the NCBInr protein database. A reference map of developing white lupin root proteins was established through 2-D gel electrophoresis and peptide mass fingerprinting. High quality peptide mass spectra were obtained for 170 proteins. Microsomal membrane proteins were separated by 1-D gel electrophoresis and identified by LC-MS/MS. A total of 74 proteins were putatively identified by the peptide mass fingerprinting and the LC-MS/MS methods. Genomic and proteomic analyses identified candidate genes and proteins encoding metal binding and/or transport proteins, transcription factors, ABC transporters and phenylpropanoid biosynthetic enzymes.ConclusionThe combined EST and protein datasets will facilitate the understanding of white lupin's response to biotic and abiotic stresses and its utility for phytoremediation. The root ESTs provided 82 perfect simple sequence repeat (SSR) markers with potential utility in breeding white lupin for enhanced agronomic traits.

Characterization of an Isoflavonoid-Specific Prenyltransferase from Lupinus albus

“…One EST (FG092841), obtained from developing roots of white lupin 'Netherland' (Tian et al, 2009), shared 35.7% and 35.7% sequence identities with SfN8DT-1 and G4DT, respectively, but higher sequence identity (96.2%) with VET2-2 (soybean homogentisate phytyltransferase). However, the expression profile of this gene did not show any obvious association with the accumulation of prenylated compounds in lupin; therefore, the gene is more likely related to the biosynthesis of vitamin E or plastoquinone that mainly occurs in the aerial parts of plants (Venkatesh et al, 2006).…”

“…From a total of about 8,000 white lupin EST sequences obtained from our own EST collection (Tian et al, 2009) and the National Center for Biotechnology Information database, two candidate ESTs were selected based on their sequence similarities with known flavonoid and isoflavonoid prenyltransferases. One EST (FG092841), obtained from developing roots of white lupin 'Netherland' (Tian et al, 2009), shared 35.7% and 35.7% sequence identities with SfN8DT-1 and G4DT, respectively, but higher sequence identity (96.2%) with VET2-2 (soybean homogentisate phytyltransferase).…”

An RNA-Seq Transcriptome Analysis of Orthophosphate-Deficient White Lupin Reveals Novel Insights into Phosphorus Acclimation in Plants

“…One of the most studied is the formation of cluster roots, which are closely spaced tertiary lateral rootlets that resemble bottle brushes (Neumann and Martinoia, 2002;Vance et al, 2003;Shane and Lambers, 2005;Neumann, 2010;Lambers et al, 2011). White lupin (Lupinus albus), which forms cluster roots, has become a model plant for the study of P i acquisition due to its exceptional ability to acquire nutrients unavailable to most other plants (Neumann and Martinoia, 2002;Vance et al, 2003;Tian et al, 2009;Zhu et al, 2009;Cheng et al, 2011aCheng et al, , 2011b. Cluster roots increase the root surface area for enhanced P i absorption and exude organic anions (Johnson et al, 1996;Massonneau et al, 2001;Sas et al, 2001;Wang et al, 2007) and acid phosphatases (Gilbert et al, 1999;Miller et al, 2001) that release P i from sparingly soluble inorganic and organic compounds.…”

Métodos e estratégias em proteômica e suas aplicações na área vegetal

“…Recentemente, o mapa proteico de raízes da leguminosa Lupinus albus foi caracterizado para identificar proteínas envolvidas na tolerância dessas plantas a substratos pobres em fósforo e também na capacidade fitorremediadora que esta leguminosa apresenta com o acúmulo de metais pesados (TIAN et al, 2009).…”