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Identification of a novel peptide motif that mediates cross‐linking of proteins to cell walls
Author(s) -
Domingo Concha,
Saurí Asunción,
Mansilla Elena,
Conejero Vicente,
Vera Pablo
Publication year - 1999
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1046/j.1365-313x.1999.00631.x
Subject(s) - cell wall , peptide sequence , biology , signal peptide , microbiology and biotechnology , cysteine , amino acid , peptide , complementary dna , cell , sequence motif , biochemistry , secondary cell wall , gene , enzyme
Summary A cDNA clone representing a member of a novel class of cell wall proteins was isolated from tobacco plants. We have designated this protein NtTLRP for tyrosine‐ and lysine‐rich protein. It is structurally related to the previously identified TLRP from tomato plants, sharing a high amino‐acid sequence similarity at the C‐terminal region. This region contains what appears to be a novel peptide motif which we call CD for cysteine‐rich domain, and which is common to several other cell‐wall proteins. By using a functional test in transgenic plants, we demonstrate that the presence of the CD domain is per se sufficient to cross‐link previously soluble proteins to the cell wall. We present evidence that NtTLRP is cross‐linked and specifically localizes to the cell wall of lignified cells. The highly localized deposition of NtTLRP in these cells indicates that this class of cell‐wall proteins may have a specialized function in the formation of xylem tissue.