Kolb F A, Malmgren C, Westhof E, Ehresmann C, Ehresmann B, Wagner E G, Romby P
An unusual structure formed by antisense-target RNA binding involves an extended kissing complex with a four-way junction and a side-by-side helical alignment Article de journal
Dans: RNA, vol. 6, no. 3, p. 311-324, 2000, ISBN: 10744017, (1355-8382 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Antisense/*metabolism RNA, Bacterial Proteins/*metabolism Base Pairing Base Sequence Binding Sites Cations, Divalent Computer Simulation Metals, Double-Stranded/metabolism RNA, Heavy/metabolism Models, Messenger/metabolism RNA, Molecular Molecular Sequence Data *Nucleic Acid Conformation RNA Stability RNA, Non-U.S. Gov't, ROMBY, Spliced Leader/metabolism Support, Unité ARN
@article{,
title = {An unusual structure formed by antisense-target RNA binding involves an extended kissing complex with a four-way junction and a side-by-side helical alignment},
author = {F A Kolb and C Malmgren and E Westhof and C Ehresmann and B Ehresmann and E G Wagner and P Romby},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=10744017},
isbn = {10744017},
year = {2000},
date = {2000-01-01},
journal = {RNA},
volume = {6},
number = {3},
pages = {311-324},
abstract = {The antisense RNA CopA binds to the leader region of the repA mRNA (target: CopT). Previous studies on CopA-CopT pairing in vitro showed that the dominant product of antisense RNA-mRNA binding is not a full RNA duplex. We have studied here the structure of CopA-CopT complex, combining chemical and enzymatic probing and computer graphic modeling. CopI, a truncated derivative of CopA unable to bind CopT stably, was also analyzed. We show here that after initial loop-loop interaction (kissing), helix propagation resulted in an extended kissing complex that involves the formation of two intermolecular helices. By introducing mutations (base-pair inversions) into the upper stem regions of CopA and CopT, the boundaries of the two newly formed intermolecular helices were delimited. The resulting extended kissing complex represents a new type of four-way junction structure that adopts an asymmetrical X-shaped conformation formed by two helical domains, each one generated by coaxial stacking of two helices. This structure motif induces a side-by-side alignment of two long intramolecular helices that, in turn, facilitates the formation of an additional intermolecular helix that greatly stabilizes the inhibitory CopA-CopT RNA complex. This stabilizer helix cannot form in CopI-CopT complexes due to absence of the sequences involved. The functional significance of the three-dimensional models of the extended kissing complex (CopI-CopT) and the stable complex (CopA-CopT) are discussed.},
note = {1355-8382
Journal Article},
keywords = {Antisense/*metabolism RNA, Bacterial Proteins/*metabolism Base Pairing Base Sequence Binding Sites Cations, Divalent Computer Simulation Metals, Double-Stranded/metabolism RNA, Heavy/metabolism Models, Messenger/metabolism RNA, Molecular Molecular Sequence Data *Nucleic Acid Conformation RNA Stability RNA, Non-U.S. Gov't, ROMBY, Spliced Leader/metabolism Support, Unité ARN},
pubstate = {published},
tppubtype = {article}
}
Wohrl B M, Ehresmann B, Keith G, Grice S F Le
Nuclease footprinting of human immunodeficiency virus reverse transcriptase/tRNA(Lys-3) complexes Article de journal
Dans: J Biol Chem, vol. 268, no. 18, p. 13617-13624, 1993, ISBN: 7685766, (0021-9258 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Anticodon Base Sequence HIV-1/*enzymology HIV-1 Reverse Transcriptase Hydrolysis Molecular Sequence Data Nucleic Acid Conformation RNA, Double-Stranded/metabolism RNA, Lys/chemistry/*metabolism RNA-Directed DNA Polymerase/*metabolism Recombinant Proteins/metabolism Ribonuclease, Non-U.S. Gov't Support, P.H.S., Pancreatic/metabolism Support, Transfer, U.S. Gov't, Unité ARN
@article{,
title = {Nuclease footprinting of human immunodeficiency virus reverse transcriptase/tRNA(Lys-3) complexes},
author = {B M Wohrl and B Ehresmann and G Keith and S F Le Grice},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=7685766},
isbn = {7685766},
year = {1993},
date = {1993-01-01},
journal = {J Biol Chem},
volume = {268},
number = {18},
pages = {13617-13624},
abstract = {Nuclease footprinting has been used to probe features of binary complexes of type 1 human immunodeficiency virus reverse transcriptase (HIV-1 RT) with both natural and synthetic preparations of its cognate replication primer, tRNA(Lys-3). In addition to heterodimeric RT (p66/p51), ribonucleoprotein complexes containing either the p66 or p51 subunit were analyzed. Footprinting experiments employed both structure- and sequence-specific nucleases. Our results indicate a similar mode of interaction for the three RT preparations tested, suggesting contact with each loop of the tRNA primer (D, anticodon, and T psi C), as well as minor perturbation of the anticodon stem. Although there is little evidence for extensive disruption of the 3'-acceptor stem. RNase A footprinting data with natural and synthetic tRNA suggests that potential base pairing between the T psi C and D loops is disrupted in the presence of RT.},
note = {0021-9258
Journal Article},
keywords = {Anticodon Base Sequence HIV-1/*enzymology HIV-1 Reverse Transcriptase Hydrolysis Molecular Sequence Data Nucleic Acid Conformation RNA, Double-Stranded/metabolism RNA, Lys/chemistry/*metabolism RNA-Directed DNA Polymerase/*metabolism Recombinant Proteins/metabolism Ribonuclease, Non-U.S. Gov't Support, P.H.S., Pancreatic/metabolism Support, Transfer, U.S. Gov't, Unité ARN},
pubstate = {published},
tppubtype = {article}
}