Tags

Type your tag names separated by a space and hit enter

Ubiquitin-proteasome-mediated degradation of S-RNase in a solanaceous cross-compatibility reaction.
Plant J. 2014 Jun; 78(6):1014-21.PJ

Abstract

Many plants have a self-incompatibility (SI) system in which the rejection of self-pollen is determined by multiple haplotypes at a single locus, termed S. In the Solanaceae, each haplotype encodes a single ribonuclease (S-RNase) and multiple S-locus F-box proteins (SLFs), which function as the pistil and pollen SI determinants, respectively. S-RNase is cytotoxic to self-pollen, whereas SLFs are thought to collaboratively recognize non-self S-RNases in cross-pollen and detoxify them via the ubiquitination pathway. However, the actual mechanism of detoxification remains unknown. Here we isolate the components of a SCF(SLF) (SCF = SKP1-CUL1-F-box-RBX1) from Petunia pollen. The SCF(SLF) polyubiquitinates a subset of non-self S-RNases in vitro. The polyubiquitinated S-RNases are degraded in the pollen extract, which is attenuated by a proteasome inhibitor. Our findings suggest that multiple SCF(SLF) complexes in cross-pollen polyubiquitinate non-self S-RNases, resulting in their degradation by the proteasome.

Authors+Show Affiliations

Graduate School of Biological Sciences, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara, 630-0192, Japan.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

24689760

Citation

Entani, Tetsuyuki, et al. "Ubiquitin-proteasome-mediated Degradation of S-RNase in a Solanaceous Cross-compatibility Reaction." The Plant Journal : for Cell and Molecular Biology, vol. 78, no. 6, 2014, pp. 1014-21.
Entani T, Kubo K, Isogai S, et al. Ubiquitin-proteasome-mediated degradation of S-RNase in a solanaceous cross-compatibility reaction. Plant J. 2014;78(6):1014-21.
Entani, T., Kubo, K., Isogai, S., Fukao, Y., Shirakawa, M., Isogai, A., & Takayama, S. (2014). Ubiquitin-proteasome-mediated degradation of S-RNase in a solanaceous cross-compatibility reaction. The Plant Journal : for Cell and Molecular Biology, 78(6), 1014-21. https://doi.org/10.1111/tpj.12528
Entani T, et al. Ubiquitin-proteasome-mediated Degradation of S-RNase in a Solanaceous Cross-compatibility Reaction. Plant J. 2014;78(6):1014-21. PubMed PMID: 24689760.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Ubiquitin-proteasome-mediated degradation of S-RNase in a solanaceous cross-compatibility reaction. AU - Entani,Tetsuyuki, AU - Kubo,Ken-ichi, AU - Isogai,Shin, AU - Fukao,Yoichiro, AU - Shirakawa,Masahiro, AU - Isogai,Akira, AU - Takayama,Seiji, Y1 - 2014/05/21/ PY - 2014/01/22/received PY - 2014/03/26/revised PY - 2014/03/28/accepted PY - 2014/4/3/entrez PY - 2014/4/3/pubmed PY - 2015/2/25/medline KW - 26S proteasome KW - Petunia hybrida KW - SCF SLF KW - Solanaceae KW - self-/non-self discrimination KW - self-incompatibility KW - ubiquitination SP - 1014 EP - 21 JF - The Plant journal : for cell and molecular biology JO - Plant J VL - 78 IS - 6 N2 - Many plants have a self-incompatibility (SI) system in which the rejection of self-pollen is determined by multiple haplotypes at a single locus, termed S. In the Solanaceae, each haplotype encodes a single ribonuclease (S-RNase) and multiple S-locus F-box proteins (SLFs), which function as the pistil and pollen SI determinants, respectively. S-RNase is cytotoxic to self-pollen, whereas SLFs are thought to collaboratively recognize non-self S-RNases in cross-pollen and detoxify them via the ubiquitination pathway. However, the actual mechanism of detoxification remains unknown. Here we isolate the components of a SCF(SLF) (SCF = SKP1-CUL1-F-box-RBX1) from Petunia pollen. The SCF(SLF) polyubiquitinates a subset of non-self S-RNases in vitro. The polyubiquitinated S-RNases are degraded in the pollen extract, which is attenuated by a proteasome inhibitor. Our findings suggest that multiple SCF(SLF) complexes in cross-pollen polyubiquitinate non-self S-RNases, resulting in their degradation by the proteasome. SN - 1365-313X UR - https://www.unboundmedicine.com/medline/citation/24689760/Ubiquitin_proteasome_mediated_degradation_of_S_RNase_in_a_solanaceous_cross_compatibility_reaction_ DB - PRIME DP - Unbound Medicine ER -