NDLI: The F-Box Protein AhSLF-S2 Physically Interacts with S-RNases That May Be Inhibited by the Ubiquitin/26S Proteasome Pathway of Protein Degradation during Compatible Pollination in Antirrhinum

Please wait, while we are loading the content...

The F-Box Protein AhSLF-S2 Physically Interacts with S-RNases That May Be Inhibited by the Ubiquitin/26S Proteasome Pathway of Protein Degradation during Compatible Pollination in Antirrhinum

Microarray Expression Analyses of Arabidopsis Guard Cells and Isolation of a Recessive Abscisic Acid Hypersensitive Protein Phosphatase 2C MutantW⃞

Plant Respiratory Burst Oxidase Homologs Impinge on Wound Responsiveness and Development in Lycopersicon esculentum W⃞

The Acyl-CoA Synthetase Encoded by LACS2 Is Essential for Normal Cuticle Development in Arabidopsis

Expression of a Nondegradable Cyclin B1 Affects Plant Development and Leads to Endomitosis by Inhibiting the Formation of a Phragmoplast

Type-A Arabidopsis Response Regulators Are Partially Redundant Negative Regulators of Cytokinin SignalingW⃞

Identification of Multivesicular Bodies as Prevacuolar Compartments in Nicotiana tabacum BY-2 CellsW⃞

Protein Phosphorylation in Amyloplasts Regulates Starch Branching Enzyme Activity and Protein–Protein Interactions

Disparate Roles for the Regulatory A Subunit Isoforms in Arabidopsis Protein Phosphatase 2A

Growth Regulators and the Control of Nucleotide Sugar Flux

A New Arabidopsis Gene, FLK, Encodes an RNA Binding Protein with K Homology Motifs and Regulates Flowering Time via FLOWERING LOCUS C W⃞

The Duplicated B-Class Heterodimer Model: Whorl-Specific Effects and Complex Genetic Interactions in Petunia hybrida Flower Development

The Melampsora lini AvrL567 Avirulence Genes Are Expressed in Haustoria and Their Products Are Recognized inside Plant Cells

The F-Box Protein ZEITLUPE Confers Dosage-Dependent Control on the Circadian Clock, Photomorphogenesis, and Flowering TimeW⃞

Corrections

Retraction

Year: 2004, Volume: 16, Issue: 2

Year: 2004, Volume: 16, Issue: 1

Year: 2003, Volume: 15

Year: 2003, Volume: 13

Year: 2002, Volume: 14

Year: 2001, Volume: 13

Year: 2000, Volume: 12

Year: 1999, Volume: 11

Year: 1998, Volume: 10

Year: 1997, Volume: 9

Year: 1996, Volume: 8

Year: 1995, Volume: 7

Year: 1994, Volume: 6

Year: 1993, Volume: 5

Year: 1992, Volume: 4

Year: 1991, Volume: 3

Year: 1990, Volume: 2

Year: 1989, Volume: 1

The F-Box Protein AhSLF-S2 Physically Interacts with S-RNases That May Be Inhibited by the Ubiquitin/26S Proteasome Pathway of Protein Degradation during Compatible Pollination in Antirrhinum

Content Provider	PubMed Central
Author	Qiao, Hong Wang, Hongyun Zhao, Lan Zhou, Junli Huang, Jian Zhang, Yansheng Xue, Yongbiao
Copyright Year	2004
Abstract	Self-incompatibility S-locus–encoded F-box (SLF) proteins have been identified in Antirrhinum and several Prunus species. Although they appear to play an important role in self-incompatible reaction, functional evidence is lacking. Here, we provide several lines of evidence directly implicating a role of AhSLF-S2 in self-incompatibility in Antirrhinum. First, a nonallelic physical interaction between AhSLF-S2 and S-RNases was demonstrated by both coimmunoprecipitation and yeast two-hybrid assays. Second, AhSLF-S2 interacts with ASK1- and CULLIN1-like proteins in Antirrhinum, and together, they likely form an Skp1/Cullin or CDC53/F-box (SCF) complex. Third, compatible pollination was specifically blocked after the treatment of the proteasomal inhibitors MG115 and MG132, but they had little effect on incompatible pollination both in vitro and in vivo, indicating that the ubiquitin/26S proteasome activity is involved in compatible pollination. Fourth, the ubiquitination level of style proteins was increased substantially after compatible pollination compared with incompatible pollination, and coimmunoprecipitation revealed that S-RNases were ubiquitinated after incubating pollen proteins with compatible but not with incompatible style proteins, suggesting that non-self S-RNases are possibly degraded by the ubiquitin/26S proteasome pathway. Fifth, the S-RNase level appeared to be reduced after 36 h of compatible pollination. Taken together, these results show that AhSLF-S2 interacts with S-RNases likely through a proposed SCFAhSLF-S2 complex that targets S-RNase destruction during compatible rather than incompatible pollination, thus providing a biochemical basis for the inhibition of pollen tube growth as observed in self-incompatible response in Antirrhinum.
Related Links	http://dx.doi.org/10.1105/tpc.017673
Ending Page	595
Page Count	14
Starting Page	582
File Format	PDF
ISSN	10404651
e-ISSN	1532298X
Journal	The Plant Cell
Issue Number	3
Volume Number	16
Language	English
Publisher	American Society of Plant Biologists
Publisher Date	2004-03-01
Access Restriction	Open
Rights Holder	American Society of Plant Biologists
Subject Keyword	Plant Science Cell Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Cell Biology Plant Science

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

The F-box protein AhSLF-S2 physically interacts with S-RNases that may be inhibited by the ubiquitin/26S proteasome pathway of protein degradation during compatible pollination in Antirrhinum.

The F-Box Protein AhSLF-S2 Controls the Pollen Function of S-RNase–Based Self-Incompatibility

The F-box protein AhSLF-S2 controls the pollen function of S-RNase-based self-incompatibility.

F-box proteins: the key to protein degradation

The F-box Protein Rcy1 Is Involved in the Degradation of Histone H3 Variant Cse4 and Genome Maintenance

The Arabidopsis F-Box Protein CORONATINE INSENSITIVE1 Is Stabilized by SCFCOI1 and Degraded via the 26S Proteasome Pathway [C] [W]

The F-box Protein FBXO25 Promotes the Proteasome-dependent Degradation of ELK-1 Protein

Inherent Asymmetry in the 26S Proteasome Is Defined by the Ubiquitin Receptor RPN13

Advances in Proteasome Enhancement by Small Molecules

The F-Box Protein AhSLF-S2 Physically Interacts with S-RNases That May Be Inhibited by the Ubiquitin/26S Proteasome Pathway of Protein Degradation during Compatible Pollination in Antirrhinum

Similar Documents

The F-box protein AhSLF-S2 physically interacts with S-RNases that may be inhibited by the ubiquitin/26S proteasome pathway of protein degradation during compatible pollination in Antirrhinum.

The F-Box Protein AhSLF-S2 Controls the Pollen Function of S-RNase–Based Self-Incompatibility

The F-box protein AhSLF-S2 controls the pollen function of S-RNase-based self-incompatibility.

F-box proteins: the key to protein degradation

The F-box Protein Rcy1 Is Involved in the Degradation of Histone H3 Variant Cse4 and Genome Maintenance

The Arabidopsis F-Box Protein CORONATINE INSENSITIVE1 Is Stabilized by SCFCOI1 and Degraded via the 26S Proteasome Pathway [C] [W]

The F-box Protein FBXO25 Promotes the Proteasome-dependent Degradation of ELK-1 Protein

Inherent Asymmetry in the 26S Proteasome Is Defined by the Ubiquitin Receptor RPN13

Advances in Proteasome Enhancement by Small Molecules

The F-Box Protein AhSLF-S2 Physically Interacts with S-RNases That May Be Inhibited by the Ubiquitin/26S Proteasome Pathway of Protein Degradation during Compatible Pollination in Antirrhinum