Molecular basis of the early events in plant–fungus interaction

Genome ◽  
1989 ◽  
Vol 31 (1) ◽  
pp. 342-349 ◽  
Author(s):  
P. E. Kolattukudy ◽  
G. K. Podila ◽  
R. Mohan

Fungal spores that land on aerial surfaces of plants first come into contact with plant cuticle. The cuticle is composed of an insoluble polyester called cutin, which is composed of hydroxy and hydroxyepoxy fatty acids and associated soluble waxes. The wax components can trigger differentiation of germinating fungal spores into infection structures. The penetration of the fungus into the plant requires enzymatic degradation of the polyester and the underlying carbohydrate barriers. The polyesterase, called cutinase, is induced by the contact with the plant surface. The small amount of cutinase carried by the spore generates a small amount of cutin monomers upon contact with the host, and the unique monomers trigger expression of the cutinase gene. This transcriptional level control can be demonstrated with isolated nuclei. Upon incubation of nuclei with cutin monomer and a soluble protein factor from the fungus, cutinase transcription is selectively activated. Structure activity relationships showed that the cutinase transcription activation required all of the structural elements of the cutin monomer. The cutinase transcript generated by the isolated nuclei was identical in size to the cutinase mRNA induced in the fungal cultures, which indicated usual initiation and termination. Fungal infection triggers defense reaction in plants. Plant peroxidases were implicated in the defense response of plants to fungal attack and stress. A highly anionic peroxidase involved in suberization of cell walls in tomato plants in response to fungal attack was cloned and sequenced. It was observed that in resistant lines of tomato the expression of this anionic peroxidase was induced 1 day earlier than in susceptible lines.Key words: cutinase, cutin monomers, pectate lyase, Fusarium solani pisi, anionic peroxidase.

2007 ◽  
Vol 388 (4) ◽  
pp. 373-380 ◽  
Author(s):  
Dmitri M. Hushpulian ◽  
Andrew A. Poloznikov ◽  
Pavel A. Savitski ◽  
Alexandra M. Rozhkova ◽  
Tatyana A. Chubar ◽  
...  

Abstract The role of the conserved glutamic acid residue in anionic plant peroxidases with regard to substrate specificity and stability was examined. A Glu141Phe substitution was generated in tobacco anionic peroxidase (TOP) to mimic neutral plant peroxidases such as horseradish peroxidase C (HRP C). The newly constructed enzyme was compared to wild-type recombinant TOP and HRP C expressed in E. coli. The Glu141Phe substitution supports heme entrapment during the refolding procedure and increases the reactivation yield to 30% compared to 7% for wild-type TOP. The mutation reduces the activity towards ABTS, o-phenylenediamine, guaiacol and ferrocyanide to 50% of the wild-type activity. No changes are observed with respect to activity for the lignin precursor substrates, coumaric and ferulic acid. The Glu141Phe mutation destabilizes the enzyme upon storage and against radical inactivation, mimicking inactivation in the reaction course. Structural alignment shows that Glu141 in TOP is likely to be hydrogen-bonded to Gln149, similar to the Glu143-Lys151 bond in Arabidopsis A2 peroxidase. Supposedly, the Glu141-Gln149 bond provides TOP with two different modes of stabilization: (1) it prevents heme dissociation, i.e., it ‘guards’ heme inside the active center; and (2) it constitutes a shield to protect the active center from solvent-derived radicals.


2007 ◽  
Vol 131 (4) ◽  
pp. 397-403 ◽  
Author(s):  
Tania Murphy ◽  
Ipsita Roy ◽  
Antony Harrop ◽  
Keith Dixon ◽  
Tajalli Keshavarz

2014 ◽  
Vol 27 (10) ◽  
pp. 1119-1131 ◽  
Author(s):  
Xiaogang Wu ◽  
Quan Zeng ◽  
Benjamin J. Koestler ◽  
Christopher M. Waters ◽  
George W. Sundin ◽  
...  

The bacterial soft rot pathogen Dickeya dadantii utilizes the type III secretion system (T3SS) to suppress host defense responses, and secretes pectate lyase (Pel) to disintegrate the plant cell wall. A transposon mutagenesis fluorescence-activated cell sorting screen was used to identify mutants with altered promoter activities of the T3SS pilus gene hrpA. Several insertion mutations, resulting in changes in hrpA expression, were mapped to a new locus, opgGH, which encodes the gene cluster responsible for osmoregulated periplasmic glucan (OPG) synthesis proteins. Our data showed that OPG was involved in T3SS and Pel regulation by altering the expression of the regulatory small RNA RsmB. Through genome searching, the mechanism of two novel regulatory components, the RcsCD-RcsB phosphorelay and CsrD on OPG and the rsmB gene, was further investigated. The Rcs phosphorelay and OPG inversely regulated rsmB at transcriptional and post-transcriptional levels, respectively. CsrD exhibited dual functionality in T3SS and Pel regulation by manipulating levels of RsmB RNA and cyclic diguanylate monophosphate (c-di-GMP). CsrD positively regulated the promoter activity of the rsmB gene but negatively controlled RsmB RNA at the post-transcriptional level via OpgGH. In addition, CsrD contains both GGDEF and EAL domains but acted as a c-di-GMP phosphodiesterase. When the expression of the csrD gene was induced, CsrD regulated T3SS expression and Pel production through controlling intracellular c-di-GMP levels.


1993 ◽  
Vol 70 (05) ◽  
pp. 800-806 ◽  
Author(s):  
C Ternisien ◽  
M Ramani ◽  
V Ollivier ◽  
F Khechai ◽  
T Vu ◽  
...  

SummaryTissue factor (TF) is a transmembrane receptor which, in association with factors VII and Vila, activates factor IX and X, thereby activating the coagulation protease cascades. In response to bacterial lipopolysaccharide (LPS) monocytes transcribe, synthesize and express TF on their surface. We investigated whether LPS-induced TF in human monocytes is mediated by protein kinase C (PKC) activation. The PKC agonists phorbol 12- myristate 13-acetate (PMA) and phorbol 12, 13 dibutyrate (PdBu) were both potent inducers of TF in human monocytes, whereas 4 alpha-12, 13 didecanoate (4 a-Pdd) had no such effect. Both LPS- and PMA-induced TF activity were inhibited, in a concentration dependent manner, by three different PKC inhibitors: H7, staurosporine and calphostin C. TF antigen determination confirmed that LPS-induced cell-surface TF protein levels decreased in parallel to TF functional activity under staurosporine treatment. Moreover, Northern blot analysis of total RNA from LPS- or PMA-stimulated monocytes showed a concentration-dependent decrease in TF mRNA levels in response to H7 and staurosporine. The decay rate of LPS-induced TF mRNA evaluated after the arrest of transcription by actinomycin D was not affected by the addition of staurosporine, suggesting that its inhibitory effect occurred at a transcriptional level. We conclude that LPS-induced production of TF and its mRNA by human monocytes are dependent on PKC activation.


1987 ◽  
Vol 114 (1) ◽  
pp. 18-26 ◽  
Author(s):  
Chohei Shigeno ◽  
Itsuo Yamamoto ◽  
Shegiharu Dokoh ◽  
Megumu Hino ◽  
Jun Aoki ◽  
...  

Abstract. We have partially purified a tumour factor capable of stimulating both bone resorption in vitro and cAMP accumulation in osteoblastic ROS 17/2 cells from three human tumours associated with humoral hypercalcaemia of malignancy. Purification of tumour factor by sequential acid urea extraction, gel filtration and cation-exchange chromatography, reverse-phase high performance liquid chromatography followed by analytical isoelectric focussing provided a basic protein (pI > 9.3) with a molecular weight of approximately 13 000 as a major component of the final preparation which retained both the two bioactivities. Bone resorbing activity and cAMP-increasing activity in purified factor correlated with each other. cAMP-increasing activity of the factor was heat- and acid-stable, but sensitive to alkaline ambient pH. Treatment with trypsin destroyed cAMP-increasing activity of the factor. Synthetic parathyroid hormone (PTH) antagonist, human PTH-(3– 34) completely inhibited the cAMP-increasing activity of the factor. The results suggest that this protein factor, having its effects on both osteoclastic and osteoblastic functions, may be involved in development of enhanced bone resorption in some patients with humoral hypercalcaemia of malignancy.


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