Home LiteratureArticle Details
PMID: 8038606 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

Characterization of a pollen-expressed receptor-like kinase gene of Petunia inflata and the activity of its encoded kinase.

The Plant cell ·Vol. 6 ·No. 5 ·1994-05-00 ·Pages 709-21

Mu JH, Lee HS, Kao TH

Abstract

From a pollen tube cDNA library of Petunia inflata, we isolated clones encoding a protein with structural features and biochemical properties characteristic of receptor-like kinases. It was designated PRK1 for pollen receptor-like kinase 1. The cytoplasmic domain of PRK1 is highly similar to the kinase domains of other plant receptor-like kinases and contains nearly all of the conserved amino acids for serine/threonine kinases. The extracellular domain of PRK1 contains leucine-rich repeats as found in some other plant receptor-like kinases, but overall its sequence in this region does not share significant similarity. Characterization of a gene encoding PRK1 revealed the presence of two introns. During pollen development, PRK1 mRNA was first detected in anthers containing mostly binucleate microspores; it reached the highest level of mature pollen and remained at a high level in in vitro-germinated pollen tubes. The recombinant cytoplasmic domain of PRK1 autophosphorylated on serine and tyrosine, suggesting that PRK1 may be a dual-specificity kinase. Monospecific immune serum to the recombinant extracellular domain of PRK1 detected a 69-kD protein in microsomal membranes of pollen and pollen tubes. The characteristics of PRK1 suggest that it may play a role in signal transduction events during pollen development and/or pollination.

Related Genes
MeSH Terms
Amino Acid Sequence Animals Base Sequence Consensus Sequence DNA Primers DNA, Complementary/metabolism Gene Library Genes, Plant Humans Molecular Sequence Data Plant Proteins Plants/enzymology,genetics Pollen Protein Serine-Threonine Kinases RNA, Messenger/biosynthesis,metabolism Receptor Protein-Tyrosine Kinases/biosynthesis,genetics,metabolism Recombinant Proteins/biosynthesis,isolation & purification,metabolism Restriction Mapping Sequence Homology, Amino Acid Signal Transduction
Chemicals
DNA Primers DNA, Complementary Plant Proteins RNA, Messenger Recombinant Proteins PRK1 protein, Petunia inflata Receptor Protein-Tyrosine Kinases Protein Serine-Threonine Kinases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Mu J H
Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park 16802.
Lee H S
Kao T H
References (32)
32 references, click to expand
  1. Lutropin-choriogonadotropin receptor: an unusual member of the G protein-coupled receptor family.
    Science. 1989 Aug 4;245(4917):494-9 PMID: 2502842
  2. Novel protein kinase of Arabidopsis thaliana (APK1) that phosphorylates tyrosine, serine and threonine.
    Plant Mol Biol. 1992 Nov;20(4):653-62 PMID: 1450380
  3. slit: an extracellular protein necessary for development of midline glia and commissural axon pathways contains both EGF and LRR domains.
    Genes Dev. 1990 Dec;4(12A):2169-87 PMID: 2176636
  4. Charge clusters and the orientation of membrane proteins.
    J Membr Biol. 1982;66(3):203-12 PMID: 6808138
  5. Cleavage of structural proteins during the assembly of the head of bacteriophage T4.
    Nature. 1970 Aug 15;227(5259):680-5 PMID: 5432063
  6. The Toll gene of Drosophila, required for dorsal-ventral embryonic polarity, appears to encode a transmembrane protein.
    Cell. 1988 Jan 29;52(2):269-79 PMID: 2449285
  7. Fission yeast p107wee1 mitotic inhibitor is a tyrosine/serine kinase.
    Nature. 1991 Feb 28;349(6312):808-11 PMID: 1825699
  8. STY, a tyrosine-phosphorylating enzyme with sequence homology to serine/threonine kinases.
    Mol Cell Biol. 1991 Jan;11(1):568-72 PMID: 1986248
  9. Signal transduction by receptors with tyrosine kinase activity.
    Cell. 1990 Apr 20;61(2):203-12 PMID: 2158859
  10. Effect on in Vitro Pollen Growth of an Isolated Style Glycoprotein Associated with Self-Incompatibility in Nicotiana alata.
    Plant Physiol. 1989 Jan;89(1):360-7 PMID: 16666539
  11. Receptor-like protein kinase genes of Arabidopsis thaliana.
    Plant J. 1993 Mar;3(3):451-6 PMID: 8220453
  12. MsERK1: a mitogen-activated protein kinase from a flowering plant.
    Plant Cell. 1993 Jan;5(1):87-96 PMID: 8439746
  13. Patterns of amino acids near signal-sequence cleavage sites.
    Eur J Biochem. 1983 Jun 1;133(1):17-21 PMID: 6852022
  14. Molecular cloning of a putative receptor protein kinase gene encoded at the self-incompatibility locus of Brassica oleracea.
    Proc Natl Acad Sci U S A. 1991 Oct 1;88(19):8816-20 PMID: 1681543
  15. Multiple cDNAs encoding the esk kinase predict transmembrane and intracellular enzyme isoforms.
    Mol Cell Biol. 1992 Jun;12(6):2681-9 PMID: 1375325
  16. A novel modular mosaic of cell adhesion motifs in the extracellular domains of the neurogenic trk and trkB tyrosine kinase receptors.
    Oncogene. 1991 Oct;6(10):1807-11 PMID: 1656363
  17. The S-locus receptor kinase gene in a self-incompatible Brassica napus line encodes a functional serine/threonine kinase.
    Plant Cell. 1992 Oct;4(10):1273-81 PMID: 1332796
  18. Expression cloning of the TGF-beta type II receptor, a functional transmembrane serine/threonine kinase.
    Cell. 1992 Feb 21;68(4):775-85 PMID: 1310899
  19. The protein kinase family: conserved features and deduced phylogeny of the catalytic domains.
    Science. 1988 Jul 1;241(4861):42-52 PMID: 3291115
  20. Drosophila chaoptin, a member of the leucine-rich repeat family, is a photoreceptor cell-specific adhesion molecule.
    EMBO J. 1990 Jun;9(6):1969-77 PMID: 2189727
  21. Cloning of the alpha chain of human platelet glycoprotein Ib: a transmembrane protein with homology to leucine-rich alpha 2-glycoprotein.
    Proc Natl Acad Sci U S A. 1987 Aug;84(16):5615-9 PMID: 3303030
  22. Structural framework for the protein kinase family.
    Annu Rev Cell Biol. 1992;8:429-62 PMID: 1335745
  23. Ablation of Papillar Cell Function in Brassica Flowers Results in the Loss of Stigma Receptivity to Pollination.
    Plant Cell. 1993 Mar;5(3):263-275 PMID: 12271063
  24. The TMK1 gene from Arabidopsis codes for a protein with structural and biochemical characteristics of a receptor protein kinase.
    Plant Cell. 1992 Oct;4(10):1263-71 PMID: 1332795
  25. An Arabidopsis serine/threonine kinase homologue with an epidermal growth factor repeat selected in yeast for its specificity for a thylakoid membrane protein.
    Proc Natl Acad Sci U S A. 1992 Nov 15;89(22):10989-92 PMID: 1438303
  26. A plant receptor-like gene, the S-locus receptor kinase of Brassica oleracea L., encodes a functional serine/threonine kinase.
    Plant Physiol. 1993 Mar;101(3):1103-6 PMID: 8310048
  27. An Arabidopsis thaliana Gene with Sequence Similarity to the S-Locus Receptor Kinase of Brassica oleracea: Sequence and Expression.
    Plant Physiol. 1992 May;99(1):284-90 PMID: 16668863
  28. Relationship of a putative receptor protein kinase from maize to the S-locus glycoproteins of Brassica.
    Nature. 1990 Jun 21;345(6277):743-6 PMID: 2163028
  29. Spk1, a new kinase from Saccharomyces cerevisiae, phosphorylates proteins on serine, threonine, and tyrosine.
    Mol Cell Biol. 1991 Feb;11(2):987-1001 PMID: 1899289
  30. The flanking regions of two Petunia inflata S alleles are heterogeneous and contain repetitive sequences.
    Plant Mol Biol. 1992 Feb;18(4):725-37 PMID: 1558946
  31. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.
    Anal Biochem. 1976 May 7;72:248-54 PMID: 942051
  32. Microtubule-associated protein 2 kinases, ERK1 and ERK2, undergo autophosphorylation on both tyrosine and threonine residues: implications for their mechanism of activation.
    Proc Natl Acad Sci U S A. 1991 Jul 15;88(14):6142-6 PMID: 1712480
Article Info
Journal
The Plant cell
Abbr.
Plant Cell
ISSN
1040-4651
Published
1994-05-00
Pages
709-21
Language
English
Region
England
NLM ID
9208688
PMCID
PMC160470
Subset
IM
Databases
GENBANK
L27341
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com