Membrane-associated NRPM proteins are novel suppressors of stomatal production in Arabidopsis.

In Arabidopsis, stomatal development and patterning require tightly regulated cell division and cell-fate differentiation that are controlled by key transcription factors and signaling molecules. To identify new regulators of stomatal development, we assay the transcriptomes of plants bearing enriched stomatal lineage cells that undergo active division. A member of the novel regulators at the plasma membrane (NRPM) family annotated as hydroxyproline-rich glycoproteins was identified to highly express in stomatal lineage cells.

A bacterial effector protein uncovers a plant metabolic pathway involved in tolerance to bacterial wilt disease.

Bacterial wilt caused by the soil-borne plant pathogen Ralstonia solanacearum is a devastating disease worldwide. Upon plant colonization, R. solanacearum replicates massively, causing plant wilting and death; collapsed infected tissues then serve as a source of inoculum.

Intra-strain Elicitation and Suppression of Plant Immunity by Type-III Effectors in .

Effector proteins delivered inside plant cells are powerful weapons for bacterial pathogens, but this exposes the pathogen to potential recognition by the plant immune system. Therefore, the effector repertoire of a given pathogen must be balanced for a successful infection. is an aggressive pathogen with a large repertoire of secreted effectors.

A bacterial effector protein prevents MAPK-mediated phosphorylation of SGT1 to suppress plant immunity.

Nucleotide-binding domain and leucine-rich repeat-containing (NLR) proteins function as sensors that perceive pathogen molecules and activate immunity. In plants, the accumulation and activation of NLRs is regulated by SUPPRESSOR OF G2 ALLELE OF skp1 (SGT1). In this work, we found that an effector protein named RipAC, secreted by the plant pathogen Ralstonia solanacearum, associates with SGT1 to suppress NLR-mediated SGT1-dependent immune responses, including those triggered by another R.

The Ralstonia solanacearum csp22 peptide, but not flagellin-derived peptides, is perceived by plants from the Solanaceae family.

Ralstonia solanacearum, the causal agent of bacterial wilt disease, is considered one of the most destructive bacterial pathogens due to its lethality, unusually wide host range, persistence and broad geographical distribution. In spite of the extensive research on plant immunity over the last years, the perception of molecular patterns from R. solanacearum that activate immunity in plants is still poorly understood, which hinders the development of strategies to generate resistance against bacterial wilt disease.

The Type III Effector RipAY Is Phosphorylated in Plant Cells to Modulate Its Enzymatic Activity.

Most bacterial pathogens subvert plant cellular functions using effector proteins delivered inside plant cells. In the plant pathogen , several of these effectors contain domains with predicted enzymatic activities, including acetyltransferases, phosphatases, and proteases, among others. How these enzymatic activities get activated inside plant cells, but not in the bacterial cell, remains unknown in most cases.

Analysis of PAMP-Triggered ROS Burst in Plant Immunity.

The plant perception of pathogen-associated molecular patterns triggers a plethora of cellular immune responses. One of these responses is a rapid and transient burst of reactive oxygen species (ROS) mediated by plasma membrane-localized NADPH oxidases. The ROS burst requires a functional receptor complex and the contribution of several additional regulatory components.

Transcriptomic Analysis of Responses to Imbalanced Carbon: Nitrogen Availabilities in Rice Seedlings.

The internal C:N balance must be tightly controlled for the normal growth and development of plants. However, the underlying mechanisms, by which plants sense and balance the intracellular C:N status correspondingly to exogenous C:N availabilities remain elusive. In this study, we use comparative gene expression analysis to identify genes that are responsive to imbalanced C:N treatments in the aerial parts of rice seedlings.

The Ralstonia solanacearum type III effector RipAY targets plant redox regulators to suppress immune responses.

The subversion of plant cellular functions is essential for bacterial pathogens to proliferate in host plants and cause disease. Most bacterial plant pathogens employ a type III secretion system to inject type III effector (T3E) proteins inside plant cells, where they contribute to the pathogen-induced alteration of plant physiology. In this work, we found that the Ralstonia solanacearum T3E RipAY suppresses plant immune responses triggered by bacterial elicitors and by the phytohormone salicylic acid.

Expression, in vivo localization and phylogenetic analysis of a pyridoxine 5'-phosphate oxidase in Arabidopsis thaliana.

Pyridoxal phosphate (PLP), a vitamin B(6) vitamer, is an essential cofactor for numerous enzymes. Pyridoxine/pyridoxamine phosphate oxidase (PPOX) catalyzes the synthesis of pyridoxal phosphate from pyridoxine phosphate (PNP) and/or pyridoxamine phosphate (PMP). The At5g49970 locus in Arabidopsis thaliana encodes an AtPPOX, a PNP/PMP oxidase.

Identification of a pyridoxine (pyridoxamine) 5'-phosphate oxidase from Arabidopsis thaliana.

Pyridoxine (pyridoxamine) 5'-phosphate oxidase (PPOX) catalyzes the oxidative conversion of pyridoxamine 5'-phosphate (PMP) or pyridoxine 5'-phosphate (PNP) to pyridoxal 5'-phosphate (PLP). The At5g49970 gene of Arabidopsis thaliana shows homology to PPOX's from a number of organisms including the Saccharomyces cerevisiae PDX3 gene. A cDNA corresponding to putative A.

Progress in the Research of Plasminogen Activator Inhibitor Type-2.

Plasminogen activator inhibitor type-2 (PAI-2) inhibits urokinase type plasminogen activator (u-PA) most specifically and high efficiently, following the mechanism of serine proteinase inhibitor (serpin) superfamily. PAI-2 plays a very important role in vivo there are, however, two conflicting views on the role of PAI-2 in cancer. Tissue-type plasminogen activator, vitronectin, transglutaminases, fibrin and many other molecules can interact with PAI-2.