Abscisic Acid Refines the Synthesis of Chloroplast Proteins in Maize (Zea mays) in Response to Drought and Light

Abstract

To better understand abscisic acid (ABA) regulation of the synthesis of chloroplast proteins in maize (Zea mays L.) in response to drought and light, we compared leaf proteome differences between maize ABA-deficient mutant vp5 and corresponding wild-type Vp5 green and etiolated seedlings exposed to drought stress. Proteins extracted from the leaves of Vp5 and vp5 seedlings were used for two-dimensional electrophoresis (2-DE) and subsequent matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry (MS). After Coomassie brilliant blue staining, approximately 450 protein spots were reproducibly detected on 2-DE gels. A total of 36 differentially expressed protein spots in response to drought and light were identified using MALDI-TOF MS and their subcellular localization was determined based on the annotation of reviewed accession in UniProt Knowledgebase and the software prediction. As a result, corresponding 13 proteins of the 24 differentially expressed protein spots were definitely localized in chloroplasts and their expression was in an ABA-dependent way, including 6 up-regulated by both drought and light, 5 up-regulated by drought but down-regulated by light, 5 up-regulated by light but down-regulated by drought; 5 proteins down-regulated by drought were mainly those involved in photosynthesis and ATP synthesis. Thus, the results in the present study supported the vital role of ABA in regulating the synthesis of drought- and/or light-induced proteins in maize chloroplasts and would facilitate the functional characterization of ABA-induced chloroplast proteins in C4 plants.

“Omics” of Maize Stress Response for Sustainable Food Production: Opportunities and Challenges

“…In maize roots, proteins associated with drought stress were primarily involved in energy and metabolism, redox homeostasis, and regulatory processes (Hu et al, 2011); in maize leaves, the identified proteins were primarily involved in processes such as ATP synthesis, protein synthesis, chlorophyll synthesis, CO 2 fixation, gluconeogenesis, antioxidant defense, and signal transduction. Most of the proteins that differentially accumulated in leaves were localized to the chloroplasts and functioned in an ABA-dependent manner in response to drought and light stress (Hu et al, 2012). These results reveal an important role of ABA in regulating the synthesis of drought-induced proteins.…”

“…As determined by omics studies, the proteins involved in the maize drought response primarily include protective proteins (such as HSPs) (Benesova et al, 2012;Hu et al, 2010a;Li et al, 2009;Luo et al, 2010), late embryogenesisabundant proteins (LEAs) (Benesova et al, 2012;Huang et al, 2012), stress response-related proteins (such as NBS-LRR resistance-like protein) (Hu et al, 2012), 14-3-3-like proteins (Huang et al, 2012;Li et al, 2009), phytohormonerelated proteins, and signaling proteins (such as auxinrepressed protein and serine/threonine protein kinase) (Bonhomme et al, 2012;Hu et al, 2011;Luo et al, 2010).…”

Identification of proteins related to microspore embryogenesis responsiveness in anther cultures of winter triticale (×Triticosecale Wittm.)

“…This protein catalyses the ATP-dependent phosphorylation of ribulose-5-phosphate to ribulose-1,5-phosphate, a key step in the pentose phosphate pathway where carbon dioxide is assimilated. Some data showed that PRK synthesis could be regulated by such factors like light, drought stress or ABA (Hu et al 2012).…”

Protein sHSP26 improves chloroplast performance under heat stress by interacting with specific chloroplast proteins in maize (Zea mays)

“…The spots were aseptically removed under a laminar flow hood. The processing of the gel plugs, trypsin digestion and MALDI-TOF-MS analysis using an Ettan MALDI-TOF Pro mass spectrometer (GE Healthcare, USA) was performed as previously described [16]. Mascot software (v2.2.03, http://www.matrixscience.com/) was used to automatically match the obtained MS/MS spectra to proteins in the NCBInr 20,121,026 databases (21,171,493 sequences; 7,255,144,311 residues; http://www.ncbi.nlm.nih.gov/).…”