Purification and characterization of a non-S-RNase and S-RNases from styles of Japanese pear (Pyrus pyrifolia)

Norioka, Shigemi; Oneyama, Chitose; Takuma, Seiji; Shinkawa, Toyohide; Ishimizu, Takeshi; Nakanishi, Tetsu; Sakiyama, Fumio

doi:10.1016/j.plaphy.2007.09.008

Cited by 14 publications

(5 citation statements)

References 33 publications

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“…A Y2H assay was performed to examine whether A14 interacts with S ‐RNases. We ligated the CDS of S 1 ‐, S 2 ‐, S 3 ‐ and S 9 ‐RNase and negative control non‐ S ‐RNase (Norioka et al ., ) from apple into the pGBKT7 vector to create fusions with the binding domain (BD) (named S 1 , S 2 , S 3 , S 9 Mat‐BD), and the CDS of A14 was similarly fused to the activation domain (AD) in the pGADT7 vector (named A14‐AD). Coexpression with A14‐AD/ S 1 ‐, S 2 ‐, S 3 ‐, S 9 ‐BD showed growth on the selective medium SD[‐Leu/‐Trp/‐His/‐Ade], whereas coexpression with A14‐AD/non‐ S ‐RNase‐BD, or other negative combinations, did not show growth on the same medium (Figs b,c, S1a), indicating that A14 interacted with the different S ‐haplotype S ‐RNases.…”

Section: Resultsmentioning

confidence: 99%

Apple S‐RNase triggers inhibition of tRNA aminoacylation by interacting with a soluble inorganic pyrophosphatase in growing self‐pollen tubes in vitro

Meng

et al. 2018

New Phytologist

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Apple exhibits S-RNase-based self-incompatibility (SI), in which S-RNase plays a central role in rejecting self-pollen. It has been proposed that the arrest of pollen growth in SI of Solanaceae plants is a consequence of the degradation of pollen rRNA by S-RNase; however, the underlying mechanism in Rosaceae is still unclear. Here, we used S -RNase as a bait to screen an apple pollen cDNA library and characterized an apple soluble inorganic pyrophosphatase (MdPPa) that physically interacted with S-RNases. When treated with self S-RNases, apple pollen tubes showed a marked growth inhibition, as well as a decrease in endogenous soluble pyrophosphatase activity and elevated levels of inorganic pyrophosphate (PPi). In addition, S-RNase was found to bind to two variable regions of MdPPa, resulting in a noncompetitive inhibition of its activity. Silencing of MdPPa expression led to a reduction in pollen tube growth. Interestingly, tRNA aminoacylation was inhibited in self S-RNase-treated or MdPPa-silenced pollen tubes, resulting in the accumulation of uncharged tRNA. Furthermore, we provide evidence showing that this disturbance of tRNA aminoacylation is independent of RNase activity. We propose an alternative mechanism differing from RNA degradation to explain the cytotoxicity of the S-RNase apple SI process.

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Section: Resultsmentioning

confidence: 99%

Apple S‐RNase triggers inhibition of tRNA aminoacylation by interacting with a soluble inorganic pyrophosphatase in growing self‐pollen tubes in vitro

Meng

et al. 2018

New Phytologist

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“…As the activity of purified S ‐RNase was lower than that of natural S ‐RNase (Norioka et al ., ), a crude protein extract from the style of Malus domestica cv. ‘Ralls Janet’ ( S 1 S 2 ) was used to culture the self‐pollen.…”

Section: Resultsmentioning

confidence: 99%

Apple MdABCF assists in the transportation of S‐RNase into pollen tubes

Meng

et al. 2014

The Plant Journal

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SUMMARYSelf-incompatibility (SI) is a reproductive isolation mechanism in flowering plants. Plants in the Solanaceae, Rosaceae and Plantaginaceae belong to the gametophytic self-incompatibility type. S-RNase, which is encoded by a female-specific gene located at the S locus, degrades RNA in the pollen tube and causes SI. Recent studies have provided evidence that S-RNase is transported non-selectively into the pollen tube, but have not specified how this transportation is accomplished. We show here that the apple (Malus domestica) MdABCF protein, which belongs to group F of the ABC transporter family, assists in transportation of S-RNase into the pollen tube. MdABCF is located in the pollen tube membrane and interacts with S-RNase. S-RNase was unable to enter the pollen tube when MdABCF was silenced by antisense oligonucleotide transfection. Our results show that MdABCF assists in transportation of either self or non-self S-RNase into the pollen tube. Moreover, MdABCF coordinates with the cytoskeleton to transport S-RNase. Blockage of S-RNase transport disrupts self-incompatibility in this system.

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“…These findings lead us to believe that the high temperature exposure caused a decrease in S-RNase activity, which enabled self-pollen tube growth in the 50°Ctreated styles of 'Somei-yoshino'. It should be noted that a reduction in RNase activity does not directly indicate a decrease in actual S-RNase activity, since protein extracts from the style also included other RNases, including so-called S-like RNases (Norioka et al, 2007;Sassa et al, 1992;Tao et al, 1997). In future studies, optimized methodologies that provide a more accurate quantification of S-RNases will improve the ability to make these determinations.…”

Section: Discussionmentioning

confidence: 99%

Decreased RNase Activity Under High Temperature Is Related to Promotion of Self-pollen Tube Growth in the Pistil of the Japanese Flowering Cherry, <i>Prunus</i> × <i>yedoensis</i> ‘Somei-yoshino’

et al. 2020

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Prunus × yedoensis Matsum. 'Somei-yoshino' is one of the most popular flowering cherry cultivars in Japan. However, because flowering cherries have strict self-incompatibility (SI), it is difficult to develop selfing families or inbred lines for breeding and genetic studies. SI in Prunus is achieved through arrest of self-pollen tube growth in the style by ribonuclease S-RNase. To determine a suitable way to overcome SI in Prunus, we examined the influence of hot water immersion on RNase activity in the style of 'Somei-yoshino'. When the styles were immersed in 20°C, 30°C, and 40°C water baths, their RNase activity was not significantly different from that of untreated styles (P > 0.05); however, it significantly decreased in styles heated in 50°C water baths (P < 0.01). Furthermore, the RNase activity decreased with an increase in the incubation time (e.g., 1, 3, and 5 min). Additionally, heat treatment at 50°C promoted the growth of self-pollen tubes in the style. Some selfpollen tubes even reached the bottom of the style. The high temperature treatment with reduced RNase activity can overcome stylar SI in Prunus.

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Purification and characterization of a non-S-RNase and S-RNases from styles of Japanese pear (Pyrus pyrifolia)

Cited by 14 publications

References 33 publications

Apple S‐RNase triggers inhibition of tRNA aminoacylation by interacting with a soluble inorganic pyrophosphatase in growing self‐pollen tubes in vitro

Apple S‐RNase triggers inhibition of tRNA aminoacylation by interacting with a soluble inorganic pyrophosphatase in growing self‐pollen tubes in vitro

Apple MdABCF assists in the transportation of S‐RNase into pollen tubes

Decreased RNase Activity Under High Temperature Is Related to Promotion of Self-pollen Tube Growth in the Pistil of the Japanese Flowering Cherry, <i>Prunus</i> × <i>yedoensis</i> ‘Somei-yoshino’

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