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This gene encodes a thaumatin-like protein[1].

Annotated Information


  This gene encodes a thaumatin-like protein. Thaumatin belongs to the pathogen response 5(PR5) family, and is only exclusively expressed in pathological
conditions such as paramicrobe infection or mechanical damage[2]. Therefore, it is thought that this protein is involved in acquired systematic resistance
and the response to biotic stress; the latter process leads to microbe growth inhibition and spore germination reduction[2]. However, the precise mechanism
in rice is unknown. In addition, this thaumatin-like peotein harbors ATP-binding potentiality and Serine/threonine-protein kinase activity according to
the homology prediction[3]. And an attractive feature of this protein is its sweet flavor, and this feature may be used in food industry[4].



  This thaumatin-like protein is derived from the rice cultivar Nipponbare[5]. The name 'thaumatin-like' from its homology with thaumatin. Thaumatin
is firstly extracted from the fruit Thaumatococcus daniellii growing in West Africa[4]. Thaumatin-like proteins are in diverse plants, and can be
isolated from Hordeum vulgare (barley), Actinidia deliciosa(kiwifruit), Zea mays (maize), Pseudotsuga menziesii (douglas-firs), Nicotiana tabacum (tobacco),
Solanum lycopersicum (tomato) and Triticum sp. (wheat) . Most of the thaumatin-like protein have a molecular weight in the range of 18 kDa to 25 kDa and
have a pH in the range from 4.5 to 5.5.[2]



  Thaumatin-like proteins appear to have originated in early eukaryotes and share a well-defined thaumatin-like protein domain[6]. Evolutionary 
relationships within the thaumatin-like protein superfamily are not well understood. For example, a study of phylogenetic and structural relationships[7],
suggested that plant PR5 proteins are paraphyletic in angiosperms and related to animal thaumatin-like proteins from insects and nematodes. However,
another study indicated that thaumatin-like proteins are grouped into three major clades representing the animal, plant, and fungal kingdoms, respectively.Alignment
analysis was done using 118 putative TLP sequences selected from ascomycete and basidiomycete fungi, moss, gymnosperms and angiosperms, plus animals as represented
by nematodes and insects. The neighbor joining algorithm was used to construct a phylogenetic tree (Fig. 3). The topological pattern of the resulting tree indicates
that the TLP superfamily is highly divergent, with the possibility of nine distinct groups (I–IX), each containing proteins with relatively high identity[8].

... Figure 1 caption Phylogenetic analysis of 118 TLPs by the neighborjoining (NJ) method[6]. ...

Labs working on this gene

1. Natural Resources Canada, Canadian Forest Service, Pacific Forestry Centre, Canada.
2. Department of Microbiology, Miami University, USA. 
3. Institute of Tropical Agriculture, Universiti Putra Malaysia, Malaysia.
4. National Institute of Crop Science, Tsukuba, Japan.
5. Institute for Plant Biology, University of Zurich, Switzerland.
6. Jayaraj Jayaraman Lab,  Department of Life Sciences, The University of the West Indies.


[1]Reimmann C, Dudler R. cDNA cloning and sequence analysis of a pathogen-induced thaumatin-like protein from rice (Oryza sativa). Plant Physiol. 1993;101(3):1113-1114.

[2]V. Borad, S. Sriram. Pathogenesis-Related Proteins for the Plant Protection. Asian J. Exp. Sci.2008;22(3):189-196.

[3]C7IXE4 (C7IXE4_ORYSJ),UniProtKB/TrEMBL:Os01g0113350 protein. [[1]]


[5]NCBI Reference Sequence: NC_008394.4:Oryza sativa Japonica Group DNA, chromosome 1, complete sequence, cultivar: Nipponbare. [[3]]

[6]Liu JJ, Sturrock R, Ekramoddoullah AK.The superfamily of thaumatin-like proteins: its origin, evolution, and expression towards biological function. Plant Cell Rep. 2010;29(5):419-36.

[7]Shatters RG Jr, Boykin LM, Lapointe SL, Hunter WB, Weathersbee AA 3rd (2006) Phylogenetic and structural relationships of the PR5 gene family reveal an ancient multigene family conserved in plants and select animal taxa. J Mol Evol 63:12–29.

[8]Sakamoto Y, Watanabe H, Nagai M, Nakade K, Takahashi M, Sato T (2006) Lentinula edodes tlg1 encodes a thaumatin-like protein that is involved in Lentinan degradation and fruiting body senescence. Plant Physiol 141:793–801

Structured Information