Brassinosteroid-independent function of BRI1 /CLV1 chimeric receptors (Record no. 48631)
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| fixed length control field | 01979nam a2200205Ia 4500 |
| 003 - CONTROL NUMBER IDENTIFIER | |
| control field | MX-MdCICY |
| 005 - DATE AND TIME OF LATEST TRANSACTION | |
| control field | 20250625153941.0 |
| 040 ## - CATALOGING SOURCE | |
| Transcribing agency | CICY |
| 090 ## - LOCALLY ASSIGNED LC-TYPE CALL NUMBER (OCLC); LOCAL CALL NUMBER (RLIN) | |
| Classification number (OCLC) (R) ; Classification number, CALL (RLIN) (NR) | B-14443 |
| 008 - FIXED-LENGTH DATA ELEMENTS--GENERAL INFORMATION | |
| fixed length control field | 250602s9999 xx |||||s2 |||| ||und|d |
| 245 10 - TITLE STATEMENT | |
| Title | Brassinosteroid-independent function of BRI1 /CLV1 chimeric receptors |
| 490 0# - SERIES STATEMENT | |
| Volume/sequential designation | Functional Plant Biology, 33(8), p.723-730, 2006 |
| 520 3# - SUMMARY, ETC. | |
| Summary, etc. | CLAVATA1 (CLV1)and BRASSINOSTEROID INSENSITIVE 1 (BRI1)belong to the leucine-rich repeat receptor-like kinase (LRR-RLK)family, comprising more than 200 members in Arabidopsis thaliana (L.)Heynh. and playing important roles in development and defence responses in many plant species (Di´evart and Clark 2003, 2004; Shiu and Bleecker 2001a, b). To dissect the mechanisms of receptor function, we assessed the ability of chimeric proteins containing regions from two different receptors to function in vivo. Using domains from the receptor-kinases CLAVATA1 and BRASSINOSTEROID INSENSITIVE1, we tested the ability of the resulting chimeric receptors to replace CLV1 function. Receptors with the BRI1 extracellular domain and CLV1 kinase domain were able to partially replace CLV1 function. Both loss-of-function and gain-of-function mutations within the BRI1 leucine-rich repeats (LRRs)altered the extent of rescue. Chimeric receptor function was unaffected by addition of either exogenous brassinosteroids (BR)or BR biosynthesis inhibitors, suggesting that the chimeric receptors function in a ligand-independent fashion.We propose that the BRI1 LRR domain drives chimeric receptor homodimerisation, and that the BRI1 LRR domain mutations influence homodimerisation efficiency independent of ligand binding. |
| 700 12 - ADDED ENTRY--PERSONAL NAME | |
| Personal name | Diévart, A. |
| 700 12 - ADDED ENTRY--PERSONAL NAME | |
| Personal name | Hymes, M.J. |
| 700 12 - ADDED ENTRY--PERSONAL NAME | |
| Personal name | Li, J. |
| 700 12 - ADDED ENTRY--PERSONAL NAME | |
| Personal name | Clark, S.E. |
| 856 40 - ELECTRONIC LOCATION AND ACCESS | |
| Uniform Resource Identifier | <a href="https://drive.google.com/file/d/1rWR4jHY4xlx6SQ7a70FhqLS7IACDgdML/view?usp=drivesdk">https://drive.google.com/file/d/1rWR4jHY4xlx6SQ7a70FhqLS7IACDgdML/view?usp=drivesdk</a> |
| Public note | Para ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx |
| 942 ## - ADDED ENTRY ELEMENTS (KOHA) | |
| Source of classification or shelving scheme | Clasificación local |
| Koha item type | Documentos solicitados |
| Lost status | Source of classification or shelving scheme | Damaged status | Not for loan | Collection | Home library | Current library | Shelving location | Date acquired | Total checkouts | Full call number | Date last seen | Price effective from | Koha item type |
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| Clasificación local | Ref1 | CICY | CICY | Documento préstamo interbibliotecario | 25.06.2025 | B-14443 | 25.06.2025 | 25.06.2025 | Documentos solicitados |