Style self-incompatibility gene products of Nicotlana alata are ribonucleases

McClure, Bruce; Häring, Volker; Ebert, Paul R.; Anderson, Marilyn A.; Simpson, Richard J.; Sakiyama, Fumio; Clarke, Adrienne E.

doi:10.1038/342955a0

Cited by 681 publications

(461 citation statements)

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“…S-RNase is a basic glycoprotein with RNase activity (McClure et al, 1989). RNase activity of S-RNase is required for the pistil to reject self-pollen Royo et al, 1994;McCubbin et al, 1997).…”

Section: Introductionmentioning

confidence: 99%

Structural and Transcriptional Analysis of the Self-Incompatibility Locus of Almond: Identification of a Pollen-Expressed F-Box Gene with Haplotype-Specific Polymorphism

et al. 2003

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Gametophytic self-incompatibility in Rosaceae, Solanaceae, and Scrophulariaceae is controlled by the S locus, which consists of an S-RNase gene and an unidentified "pollen S " gene. An ‫ف‬ 70-kb segment of the S locus of the rosaceous species almond, the S haplotype-specific region containing the S-RNase gene, was sequenced completely. This region was found to contain two pollen-expressed F-box genes that are likely candidates for pollen S genes. One of them, named SFB ( S haplotype-specific F-box protein), was expressed specifically in pollen and showed a high level of S haplotype-specific sequence polymorphism, comparable to that of the S-RNases. The other is unlikely to determine the S specificity of pollen because it showed little allelic sequence polymorphism and was expressed also in pistil. Three other S haplotypes were cloned, and the pollen-expressed genes were physically mapped. In all four cases, SFBs were linked physically to the S-RNase genes and were located at the S haplotype-specific region, where recombination is believed to be suppressed, suggesting that the two genes are inherited as a unit. These features are consistent with the hypothesis that SFB is the pollen S gene. This hypothesis predicts the involvement of the ubiquitin/26S proteasome proteolytic pathway in the RNase-based gametophytic self-incompatibility system.

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Section: Introductionmentioning

confidence: 99%

Structural and Transcriptional Analysis of the Self-Incompatibility Locus of Almond: Identification of a Pollen-Expressed F-Box Gene with Haplotype-Specific Polymorphism

et al. 2003

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“…Box 50, Auckland, New Zealand. S RNases (McClure et al, 1989). These glycoproteins are very abundant in the extracellular matrix of the transmitting tract and are also expressed in the stigma and in the epidermis of the placenta (Cornish et Anderson et al, 1989;McClure et al, 1993).…”

Section: Introductionmentioning

confidence: 99%

“…S allele-specific pollen rejection occurs as pollen tubes grow through the extracellular matrix of the stylar transmitting tract (Newbigin et al, 1993). The products of the S locus in the style are the To whom correspondence should be addressed.S RNases (McClure et al, 1989). These glycoproteins are very abundant in the extracellular matrix of the transmitting tract and are also expressed in the stigma and in the epidermis of the placenta (Cornish et Anderson et al, 1989;McClure et al, 1993).…”

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confidence: 99%

S RNase and Interspecific Pollen Rejection in the Genus Nicotiana: Multiple Pollen-Rejection Pathways Contribute to Unilateral Incompatibility between Self-Incompatible and Self-Compatible Species.

et al. 1996

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In self-incompatible (SI) plants, the S locus acts to prevent growth of self-pollen and thus promotes outcrossing within the species. lnterspecific crosses between SI and self-compatible (SC) species often show unilateral lncompatibility that follows the S I x SC rule: S I specles reject pollen from SC specles, but the reciproca1 crosses are usually compatible. The general validity of the S I x SC rule suggests a link between S I and interspeclflc pollen rejectlon; however, this link has been questioned because of a number of exceptlons to the rule. To clarlfy the role of the S locus in interspecific pollen rejection, we transformed severa1 Nicotlana species and hybrids with genes encodlng S A~ or SC,O RNase from S I N. alata. Compatibillty phenotypes in the transgenlc plants were tested using pollen from three SC specles showing unilateral incompatibility with N. alata. S RNase was lmpllcated ln rejecting pollen from all three specles. Rejection of N. plumbaginifolia pollen was similar to S allele-speclfic pollen rejection, showing a requirement for both S RNase and other genetic factors from N. alata. In contrast, S RNase-dependent rejectlon of N. glutinosa and N. tabacum pollen proceeded without these additional factors. N. alata also rejects pollen fmm the latter two specles through an S RNaseindependent mechanism. Our results lmplicate the S locus in all three systems, but lt 1s clear that multlple mechanisms contribute to interspecific pollen rejectlon. INTRODUCTIONMany plants have evolved genetically controlled selfincompatibility (SI) systems that promote outcrossing by restricting pollination between closely related individuals of the same species (de Nettancourt, 1977). Mechanisms also exist to restrict pollination between different species, but comparatively little is known about the control of interspecific pollination.As in other solanaceous plants, SI in the genus Nicotiana is controlled by a single multiallelic locus, the S locus (Newbigin et al., 1993). These plants employ a gametophytic SI system in which pollen is rejected if the S allele in the haploid pollen is the same as either S allele in the diploid pistil. S allele-specific pollen rejection occurs as pollen tubes grow through the extracellular matrix of the stylar transmitting tract (Newbigin et al., 1993). The products of the S locus in the style are the To whom correspondence should be addressed.S RNases (McClure et al., 1989). These glycoproteins are very abundant in the extracellular matrix of the transmitting tract and are also expressed in the stigma and in the epidermis of the placenta (Cornish et Anderson et al., 1989;McClure et al., 1993). S RNases are essential for S allele-specific pollen rejection Murfett et al., 1994), and their ribonuclease activity is required for this function . Following incompatible pollinations, RNA in selfpollen tubes is degraded, and this degradation is consistent with a cytotoxic model for pollen rejection (McClure et al., 1990;Gray et al., 1991; Dickinson, 1994). SI is therefore an active process i...

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“…21, Japan, 10%), local homology around the essential residues is fairly high. It was predicted that the glyeoprotein must have the RNase specific activity [8], and in fact McClure et al [9] reported that glycoproteins isolated from style extracts of Nicotiana ctlata exhibited ribonuclease activities. Therefore, it seems that this new class of RNase involving RNase Rh.…”

Section: Introductionmentioning

confidence: 99%

Crystal and molecular structure of RNase Rh, a new class of microbial ribonuclease from Rhizopus niveus

et al. 1992

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The crystal structure of RNase Rh, a new class of microbial ribonuelease from Rhi'.opus niveus, has been determined at 2.5 A resolution by the multiple isomorphous replacament method. The crystal structure was refined by simulated annealing with molecular dynamics. The current crystallographic R-t'actor is 0,200 in the 10-2.5 A resolution range, The molecular structure which is completely different from the known sh'uctures of RNase A and RNase T~ consists of six e~.heliees and seven//.strands, belonging to the cc+~ type structure, Two histidine and one glutamie acid resid ues which were predicted as rite most probably functional residues by chemical modification studies are Ibund to be clustered, The sterie nature of the active site taken together with the relevant site.directed mutagenesis experiments (lrie ¢t al,) indicates that: (i) the two histidine residues are the general acid and base: and (it) an aspartic acid residue plays a role of recognizing adenine moiety of the suhstrate. . The enzyme consists of a single polypeptide chain (Air,. 24,000) of" 222 amino acid residues, the sequence of which has been determined by Horiuchi et al. [5].As shown in Fig. 1, the locations of the ten halfcystines of RNase gh are almost the same as in gNase T 2 and RNase M, and the sequences around the two histidine and one glutamic acid residues that are suggested to be involved in the active site by Irie [6] are fairly well conserved. The lowest line of Fig. 1 is the sequence of S2-allelic glycoprotein of Nicotiana alata [7]. It is well known that this kind of glycoprotein is involved in self-incompatibility in flowering plants. Although overall homology between Sa-glycoprotein and the family ofRNase Rh, T2 and M is rather poor (about Abbreviations: RNase, ribonuclease; r.m.s,, root.mean.square.

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Style self-incompatibility gene products of Nicotlana alata are ribonucleases

Cited by 681 publications

References 12 publications

Structural and Transcriptional Analysis of the Self-Incompatibility Locus of Almond: Identification of a Pollen-Expressed F-Box Gene with Haplotype-Specific Polymorphism

Structural and Transcriptional Analysis of the Self-Incompatibility Locus of Almond: Identification of a Pollen-Expressed F-Box Gene with Haplotype-Specific Polymorphism

S RNase and Interspecific Pollen Rejection in the Genus Nicotiana: Multiple Pollen-Rejection Pathways Contribute to Unilateral Incompatibility between Self-Incompatible and Self-Compatible Species.

Crystal and molecular structure of RNase Rh, a new class of microbial ribonuclease from Rhizopus niveus

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