000			02025nam a2200277Ia 4500
003			MX-MdCICY
005			20260521091709.0
040			_cCICY
090			_aB-19679
245	1	0	_aStructure-function analysis reveals Trichoderma virens Tsp1 to be a novel fungal effector protein modulating plant defence
490	0		_vInternational Journal of Biological Macromolecules, 191, p.267-276, 2021
520	3		_aTrichoderma virens colonizes roots and develops a symbiotic relationship with plants where the fungal partner derives nutrients from plants and offers defence, in return. Tsp1, a small secreted cysteine-rich protein, was earlier found to be upregulated in co-cultivation of T. virens with maize roots. Tsp1 is well conserved in Ascomycota division of fungi, but none of its homologs have been studied yet. We have expressed and purified recombinant Tsp1, and resolved its structure to 1.25 Å resolutions, from two crystal forms, using Se-SAD methods. The Tsp1 adopts a ? barrel fold and forms dimer in structure as well as in solution form. DALI based structure analysis revealed the structure similarity with two known fungal effector proteins: Alt a1 and PevD1. Structure and evolutionary analysis suggested that Tsp1 belongs to a novel effector protein family. Tsp1 acted as an inducer of salicylic acid mediated susceptibility in plants, rendering maize plants more susceptible to a necrotrophic pathogen Cochliobolus heterostrophus, as observed using plant defence assay and RT-qPCR analysis.
650	1	4	_aBETA-BARREL FOLD PROTEIN
650	1	4	_aEFFECTOR
650	1	4	_aSYMBIOSIS
650	1	4	_aTRICHODERMA
650	1	4	_aTSP1
700	1	2	_aGupta, G. D.
700	1	2	_aBansal, R.
700	1	2	_aMistry, H.
700	1	2	_aPandey, B.
700	1	2	_aMukherjee, P. K.
856	4	0	_uhttps://drive.google.com/file/d/1IS3S3xLbdJi0hSIimPcQp4cg6CuEZ1-r/view?usp=drivesdk _zPara ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx
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