A pollen tube growth stimulatory glycoprotein is deglycosylated by pollen tubes and displays a glycosylation gradient in the flower

Article Abstract:

The pollen and the pistil are the two parts of the flower involved in plant sexual reproduction. The TTS protein-bound sugar gradient helps in guiding the pollen tubes from the stigma to the ovary, follwing the direction of pollen tube growth. TTS proteins adhere to the pollen tube surface and tips, and they are deglycosylated by pollen tubes when incorporated into the pollen tube walls. TTS proteins display a gradient of increasing glycosylation from the stigmatic end to the ovarian end of the style within the transmitting tissue.

Glycosylation

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NMR structure and mutagenesis of the N-terminal Dbl homology domain of the nucleotide exchange factor trio

Article Abstract:

Rho family GTPase guanine nucleotide exchange factors have a Dbl homology (DH) domain, which mediates catalysis and a pleckstrin homology (PH) domain of unknown function. The solution structure of the N-terminal DH domain of Trio, catalyzing nucleotide exchange for Rac1, is described. The structure of the all-alpha-helical protein is different to other exchange factors. Highly conserved functionally important residues of the DH domain were identified.

Observations, Nucleotides, Mutagenesis, Rho(D) immune globulin

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A floral transmitting tissue-specific glycoprotein attracts pollen tubes and stimulates their growth

Article Abstract:

The glycoprotein, TTS, purified from the tobacco stylar transmitting tissue is identified as a pistil component which supports the growth of the pollen tube between the stigma and the ovary. TTS proteins stimulate pollen tube growth in vitro and attract pollen tubes grown in a semi-in vivo culture system.

Usage

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