• Interaction

    AccNo. 54969 Score 0.49
    Name PM_9371850
    Kd 1.0

    Peptide

    AccNo. 54847
    Name YIYTQ
    Sequence YIYTQ
    54847_small
    Internalized no
    Is Motif no

    Interactor

    AccNo. 54469
    Name unknown

    Experiment

    AccNo. 54810
    Classification incorrect?
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    Voting_motivation
    CA CVD DM APO ANG MI BD
    0.78 0.48 0.21 0.32 0.30 0.19 0.39 Vote
    plus plus plus plus plus plus plus Yes
    minus minus minus minus minus minus minus No
    Name PM_9371850
    Detection unspecified method, MI:0686
    Source Pubmed Text Id 9371850
    Journal Proc Natl Acad Sci U S A. 1997 Nov 25;94(24):13357-62.
    Title Phytosulfokine-alpha, a sulfated pentapeptide, stimulates the proliferation of rice cells by means of specific high- and low-affinity binding sites.
    Authors Matsubayashi Y, Takagi L, Sakagami Y
    Text Peptide growth factors were isolated from conditioned medium derived from rice (Oryza sativa L.) suspension cultures and identified to be a sulfated pentapeptide [H-Tyr(SO3H)-Ile-Tyr(SO3H)-Thr-Gln-OH] and its C-terminal-truncated tetrapeptide [H-Tyr(SO3H)-Ile-Tyr(SO3H)-Thr-OH]. These structures were identical to the phytosulfokines originally found in asparagus (Asparagus officinalis L.) mesophyll cultures. The pentapeptide [phytosulfokine-alpha (PSK-alpha)] very strongly stimulated colony formation of rice protoplasts at concentrations above 10(-8) M, indicating a similar mode of action in rice of phytosulfokines. Binding assays using 35S-labeled PSK-alpha demonstrated the existence of both high- and low-affinity specific saturable binding sites on the surface of rice cells in suspension. Analysis of [35S]PSK-alpha binding in differential centrifugation fractions suggested association of the binding with a plasma membrane-enriched fraction. The apparent Kd values for [35S]PSK-alpha binding were found to be 1 x 10(-9) M for the high-affinity type and 1 x 10(-7) M for the low-affinity type, with maximal numbers of binding sites of 1 x 10(4) sites per cell and 1 x 10(5) sites per cell, respectively. Competition studies with [35S]PSK-alpha and several synthetic PSK-alpha analogs demonstrated that only peptides that possesses mitogenic activity can effectively displace the radioligand. These results suggest that a signal transduction pathway mediated by peptide factors is involved in plant cell proliferation.
    Mesh Terms Binding Sites; Cell Division/drug effects; Chromatography, High Pressure Liquid; Culture Media, Conditioned; Mass Spectrometry/methods; Oryza sativa/cytology; Plant Growth Regulators/pharmacology; Plant Proteins/pharmacology; Sulfur Radioisotopes