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Plant Physiol, April 2001, Vol. 125, pp. 2095-2103
A Pollen Coat Protein, SP11/SCR, Determines the Pollen
S-Specificity in the Self-Incompatibility of
Brassica Species1
Hiroshi
Shiba,
Seiji
Takayama,
Megumi
Iwano,
Hiroko
Shimosato,
Miyuki
Funato,
Tomofumi
Nakagawa,
Fang-Sik
Che,
Go
Suzuki,
Masao
Watanabe,
Kokichi
Hinata, and
Akira
Isogai*
Graduate School of Biological Sciences, Nara Institute of Science
and Technology, Ikoma 630-0101, Japan (H.S., S.T., M.I., H.S., M.F.,
T.N., F.-S.C., A.I.); Division of Natural Science, Osaka Kyoiku
University, Osaka 582-8582, Japan (G.S.); Faculty of Agriculture,
Iwate University, Morioka 020-8550, Japan (M.W.); and Research
Institute of Seed Production Company, Sendai 989-3204, Japan
(K.H.)
Many flowering plants have evolved self-incompatibility (SI)
systems to prevent inbreeding. In the Brassicaceae, SI is genetically controlled by a single polymorphic locus, termed the
S-locus. Pollen rejection occurs when stigma and pollen
share the same S-haplotype. Recognition of
S-haplotype specificity has recently been shown to
involve at least two S-locus genes,
S-receptor kinase (SRK) and
S-locus protein 11 or S-locus Cys-rich
(SP11/SCR). SRK encodes a polymorphic
membrane-spanning protein kinase, which is the sole female determinant
of the S-haplotype specificity. SP11/SCR
encodes a highly polymorphic Cys-rich small basic protein specifically
expressed in the anther tapetum and in pollen. In cauliflower
(B. oleracea), the gain-of-function approach has
demonstrated that an allele of SP11/SCR
encodes the male determinant of S-specificity. Here we
examined the function of two alleles of SP11/SCR of
B. rapa by the same approach and further established
that SP11/SCR is the sole male determinant of SI in the genus
Brassica sp. Our results also suggested that the 522-bp
5'-upstream region of the S9-SP11 gene used to drive
the transgene contained all the regulatory elements required for the
unique sporophytic/gametophytic expression observed for the native
SP11 gene. Promoter deletion analyses suggested that the
highly conserved 192-bp upstream region was sufficient for driving this
unique expression. Furthermore, immunohistochemical analyses revealed
that the protein product of the SP11 transgene was
present in the tapetum and pollen, and that in pollen of late developmental stages, the SP11 protein was mainly localized in the
pollen coat, a finding consistent with its expected biological role.
1
This work was supported in part by Grants-in-Aid
for Special Research on Priority Areas B (no. 11238025), Scientific
Research B (nos. 0948015 and 11460056), and Scientific Research on
Priority Areas (c; "Genome Biology") from the Ministry of
Education, Science, Sports and Culture, Japan.
*
Corresponding author; e-mail isogai{at}bs.aist-nara.ac.jp; fax
81-743-72-5459.
© 2001 American Society of Plant Physiologists
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