A conformational switch in the DiGIR1 ribozyme involved in release and folding of the downstream I-DirI mRNA

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Standard

A conformational switch in the DiGIR1 ribozyme involved in release and folding of the downstream I-DirI mRNA. / Nielsen, Henrik; Einvik, Christer; Lentz, Thomas E; Hedegaard, Mads Marquardt; Johansen, Steinar D.

I: RNA: A publication of the RNA Society, Bind 15, Nr. 5, 2009, s. 958-67.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Nielsen, H, Einvik, C, Lentz, TE, Hedegaard, MM & Johansen, SD 2009, 'A conformational switch in the DiGIR1 ribozyme involved in release and folding of the downstream I-DirI mRNA', RNA: A publication of the RNA Society, bind 15, nr. 5, s. 958-67. https://doi.org/10.1261/rna.669209

APA

Nielsen, H., Einvik, C., Lentz, T. E., Hedegaard, M. M., & Johansen, S. D. (2009). A conformational switch in the DiGIR1 ribozyme involved in release and folding of the downstream I-DirI mRNA. RNA: A publication of the RNA Society, 15(5), 958-67. https://doi.org/10.1261/rna.669209

Vancouver

Nielsen H, Einvik C, Lentz TE, Hedegaard MM, Johansen SD. A conformational switch in the DiGIR1 ribozyme involved in release and folding of the downstream I-DirI mRNA. RNA: A publication of the RNA Society. 2009;15(5):958-67. https://doi.org/10.1261/rna.669209

Author

Nielsen, Henrik ; Einvik, Christer ; Lentz, Thomas E ; Hedegaard, Mads Marquardt ; Johansen, Steinar D. / A conformational switch in the DiGIR1 ribozyme involved in release and folding of the downstream I-DirI mRNA. I: RNA: A publication of the RNA Society. 2009 ; Bind 15, Nr. 5. s. 958-67.

Bibtex

@article{edcd4a70388a11de87b8000ea68e967b,
title = "A conformational switch in the DiGIR1 ribozyme involved in release and folding of the downstream I-DirI mRNA",
abstract = "DiGIR1 is a group I-like cleavage ribozyme found as a structural domain within a nuclear twin-ribozyme group I intron. DiGIR1 catalyzes cleavage by branching at an Internal Processing Site (IPS) leading to formation of a lariat cap at the 5'-end of the 3'-cleavage product. The 3'-cleavage product is subsequently processed into an mRNA encoding a homing endonuclease. By analysis of combinations of 5'- and 3'-deletions, we identify a hairpin in the 5'-UTR of the mRNA (HEG P1) that is formed by conformational switching following cleavage. The formation of HEG P1 inhibits the reversal of the branching reaction, thus giving it directionality. Furthermore, the release of the mRNA is a consequence of branching rather than hydrolytic cleavage. A model is put forward that explains the release of the I-DirI mRNA with a lariat cap and a structured 5'-UTR as a direct consequence of the DiGIR1 branching reaction. The role of HEG P1 in GIR1 branching is reminiscent of that of hairpin P-1 in splicing of the Tetrahymena rRNA group I intron and illustrates a general principle in RNA-directed RNA processing.",
author = "Henrik Nielsen and Christer Einvik and Lentz, {Thomas E} and Hedegaard, {Mads Marquardt} and Johansen, {Steinar D}",
year = "2009",
doi = "10.1261/rna.669209",
language = "English",
volume = "15",
pages = "958--67",
journal = "RNA",
issn = "1355-8382",
publisher = "Cold Spring Harbor Laboratory Press",
number = "5",

}

RIS

TY - JOUR

T1 - A conformational switch in the DiGIR1 ribozyme involved in release and folding of the downstream I-DirI mRNA

AU - Nielsen, Henrik

AU - Einvik, Christer

AU - Lentz, Thomas E

AU - Hedegaard, Mads Marquardt

AU - Johansen, Steinar D

PY - 2009

Y1 - 2009

N2 - DiGIR1 is a group I-like cleavage ribozyme found as a structural domain within a nuclear twin-ribozyme group I intron. DiGIR1 catalyzes cleavage by branching at an Internal Processing Site (IPS) leading to formation of a lariat cap at the 5'-end of the 3'-cleavage product. The 3'-cleavage product is subsequently processed into an mRNA encoding a homing endonuclease. By analysis of combinations of 5'- and 3'-deletions, we identify a hairpin in the 5'-UTR of the mRNA (HEG P1) that is formed by conformational switching following cleavage. The formation of HEG P1 inhibits the reversal of the branching reaction, thus giving it directionality. Furthermore, the release of the mRNA is a consequence of branching rather than hydrolytic cleavage. A model is put forward that explains the release of the I-DirI mRNA with a lariat cap and a structured 5'-UTR as a direct consequence of the DiGIR1 branching reaction. The role of HEG P1 in GIR1 branching is reminiscent of that of hairpin P-1 in splicing of the Tetrahymena rRNA group I intron and illustrates a general principle in RNA-directed RNA processing.

AB - DiGIR1 is a group I-like cleavage ribozyme found as a structural domain within a nuclear twin-ribozyme group I intron. DiGIR1 catalyzes cleavage by branching at an Internal Processing Site (IPS) leading to formation of a lariat cap at the 5'-end of the 3'-cleavage product. The 3'-cleavage product is subsequently processed into an mRNA encoding a homing endonuclease. By analysis of combinations of 5'- and 3'-deletions, we identify a hairpin in the 5'-UTR of the mRNA (HEG P1) that is formed by conformational switching following cleavage. The formation of HEG P1 inhibits the reversal of the branching reaction, thus giving it directionality. Furthermore, the release of the mRNA is a consequence of branching rather than hydrolytic cleavage. A model is put forward that explains the release of the I-DirI mRNA with a lariat cap and a structured 5'-UTR as a direct consequence of the DiGIR1 branching reaction. The role of HEG P1 in GIR1 branching is reminiscent of that of hairpin P-1 in splicing of the Tetrahymena rRNA group I intron and illustrates a general principle in RNA-directed RNA processing.

U2 - 10.1261/rna.669209

DO - 10.1261/rna.669209

M3 - Journal article

C2 - 19329537

VL - 15

SP - 958

EP - 967

JO - RNA

JF - RNA

SN - 1355-8382

IS - 5

ER -

ID: 12127869