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פותח על ידי קלירמאש פתרונות בע"מ -
CRS1, a chloroplast group II intron splicing factor, promotes intron folding through specific interactions with two intron domains
Year:
2005
Source of publication :
Plant Cell
Authors :
אוסטרזצר, אורן
;
.
Volume :
17
Co-Authors:
Ostersetzer, O., Department of Biology, Institute of Molecular Biology, University of Oregon, Eugene, OR 97403, United States, Agricultural Research Organization, Volcani Center, Bet-Dagan 50250, Israel
Cooke, A.M., Department of Biology, Institute of Molecular Biology, University of Oregon, Eugene, OR 97403, United States
Watkins, K.P., Department of Biology, Institute of Molecular Biology, University of Oregon, Eugene, OR 97403, United States
Barkan, A., Department of Biology, Institute of Molecular Biology, University of Oregon, Eugene, OR 97403, United States
Facilitators :
From page:
241
To page:
255
(
Total pages:
15
)
Abstract:
Group II introns are ribozymes that catalyze a splicing reaction with the same chemical steps as spliceosome-mediated splicing. Many group II introns have lost the capacity to self-splice while acquiring compensatory interactions with host-derived protein cofactors. Degenerate group II introns are particularly abundant in the organellar genomes of plants, where their requirement for nuclear-encoded splicing factors provides a means for the integration of nuclear and organellar functions. We present a biochemical analysis of the interactions between a nuclear-encoded group II splicing factor and its chloroplast intron target. The maize (Zea mays) protein Chloroplast RNA Splicing 1 (CRS1) is required specifically for the splicing of the group II intron in the chloroplast atpF gene and belongs to a plant-specific protein family defined by a recently recognized RNA binding domain, the CRM domain. We show that CRS1's specificity for the atpF intron in vivo can be explained by CRS1's intrinsic RNA binding properties. CRS1 binds in vitro with high affinity and specificity to atpF intron RNA and does so through the recognition of elements in intron domains I and IV. These binding sites are not conserved in other group II introns, accounting for CRS1's intron specificity. In the absence of CRS1, the atpF intron has little uniform tertiary structure even at elevated [Mg2+]. CRS1 binding reorganizes the RNA, such that intron elements expected to be at the catalytic core become less accessible to solvent. We conclude that CRS1 promotes the folding of its group II intron target through tight and specific interactions with two peripheral intron segments. © 2004 American Society of Plant Biologists.
Note:
Related Files :
biosynthesis
enzymes
Genetics
metabolism
Nucleic acids
Plants
proteins
RNA
Zea mays
עוד תגיות
תוכן קשור
More details
DOI :
10.1105/tpc.104.027516
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
29855
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:50
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Scientific Publication
CRS1, a chloroplast group II intron splicing factor, promotes intron folding through specific interactions with two intron domains
17
Ostersetzer, O., Department of Biology, Institute of Molecular Biology, University of Oregon, Eugene, OR 97403, United States, Agricultural Research Organization, Volcani Center, Bet-Dagan 50250, Israel
Cooke, A.M., Department of Biology, Institute of Molecular Biology, University of Oregon, Eugene, OR 97403, United States
Watkins, K.P., Department of Biology, Institute of Molecular Biology, University of Oregon, Eugene, OR 97403, United States
Barkan, A., Department of Biology, Institute of Molecular Biology, University of Oregon, Eugene, OR 97403, United States
CRS1, a chloroplast group II intron splicing factor, promotes intron folding through specific interactions with two intron domains
Group II introns are ribozymes that catalyze a splicing reaction with the same chemical steps as spliceosome-mediated splicing. Many group II introns have lost the capacity to self-splice while acquiring compensatory interactions with host-derived protein cofactors. Degenerate group II introns are particularly abundant in the organellar genomes of plants, where their requirement for nuclear-encoded splicing factors provides a means for the integration of nuclear and organellar functions. We present a biochemical analysis of the interactions between a nuclear-encoded group II splicing factor and its chloroplast intron target. The maize (Zea mays) protein Chloroplast RNA Splicing 1 (CRS1) is required specifically for the splicing of the group II intron in the chloroplast atpF gene and belongs to a plant-specific protein family defined by a recently recognized RNA binding domain, the CRM domain. We show that CRS1's specificity for the atpF intron in vivo can be explained by CRS1's intrinsic RNA binding properties. CRS1 binds in vitro with high affinity and specificity to atpF intron RNA and does so through the recognition of elements in intron domains I and IV. These binding sites are not conserved in other group II introns, accounting for CRS1's intron specificity. In the absence of CRS1, the atpF intron has little uniform tertiary structure even at elevated [Mg2+]. CRS1 binding reorganizes the RNA, such that intron elements expected to be at the catalytic core become less accessible to solvent. We conclude that CRS1 promotes the folding of its group II intron target through tight and specific interactions with two peripheral intron segments. © 2004 American Society of Plant Biologists.
Scientific Publication
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