Structural features of U6 snRNA and dynamic interactions with other spliceosomal components leading to pre-mRNA splicing

T. Forné; E. Labourier; E. Antoine; F. Rossi; I. Gallouzi; G. Cathala; J. Tazi; C. Brunel

doi:10.1016/0300-9084(96)84750-X

Structural features of U6 snRNA and dynamic interactions with other spliceosomal components leading to pre-mRNA splicing

T. Forné, E. Labourier, E. Antoine, F. Rossi, I. Gallouzi, G. Cathala, J. Tazi, C. Brunel

Research output: Contribution to journal › Article › peer-review

11 Scopus citations

Abstract

In the spliceosome, the pre-mRNA, U2 and U6 snRNAs fold into a catalytic structure exhibiting striking similarities with domain V and VI of group II introns. Building of this tripartite structure implies that an evolutionary conserved base pairing between U4 and U6 snRNAs should be disrupted to allow potentially U6 catalytic residue to interact with U2 snRNAs and the pre-mRNA. The steps leading to U4/U6 disruption have been recently discovered and have been shown to involve a modification of the 3' end of U6 snRNA and the hnRNP C protein.

Original language	English (US)
Pages (from-to)	436-442
Number of pages	7
Journal	Biochimie
Volume	78
Issue number	6
DOIs	https://doi.org/10.1016/0300-9084(96)84750-X
State	Published - Jan 1 1996
Externally published	Yes

ASJC Scopus subject areas

Biochemistry

Access to Document

10.1016/0300-9084(96)84750-X

Cite this

@article{553f7153c36a4d098bb8ed44f40dea8b,

title = "Structural features of U6 snRNA and dynamic interactions with other spliceosomal components leading to pre-mRNA splicing",

abstract = "In the spliceosome, the pre-mRNA, U2 and U6 snRNAs fold into a catalytic structure exhibiting striking similarities with domain V and VI of group II introns. Building of this tripartite structure implies that an evolutionary conserved base pairing between U4 and U6 snRNAs should be disrupted to allow potentially U6 catalytic residue to interact with U2 snRNAs and the pre-mRNA. The steps leading to U4/U6 disruption have been recently discovered and have been shown to involve a modification of the 3' end of U6 snRNA and the hnRNP C protein.",

author = "T. Forn{\'e} and E. Labourier and E. Antoine and F. Rossi and I. Gallouzi and G. Cathala and J. Tazi and C. Brunel",

note = "Generated from Scopus record by KAUST IRTS on 2022-09-13",

year = "1996",

month = jan,

day = "1",

doi = "10.1016/0300-9084(96)84750-X",

language = "English (US)",

volume = "78",

pages = "436--442",

journal = "Biochimie",

issn = "0300-9084",

publisher = "Elsevier B.V.",

number = "6",

}

TY - JOUR

T1 - Structural features of U6 snRNA and dynamic interactions with other spliceosomal components leading to pre-mRNA splicing

AU - Forné, T.

AU - Labourier, E.

AU - Antoine, E.

AU - Rossi, F.

AU - Gallouzi, I.

AU - Cathala, G.

AU - Tazi, J.

AU - Brunel, C.

N1 - Generated from Scopus record by KAUST IRTS on 2022-09-13

PY - 1996/1/1

Y1 - 1996/1/1

N2 - In the spliceosome, the pre-mRNA, U2 and U6 snRNAs fold into a catalytic structure exhibiting striking similarities with domain V and VI of group II introns. Building of this tripartite structure implies that an evolutionary conserved base pairing between U4 and U6 snRNAs should be disrupted to allow potentially U6 catalytic residue to interact with U2 snRNAs and the pre-mRNA. The steps leading to U4/U6 disruption have been recently discovered and have been shown to involve a modification of the 3' end of U6 snRNA and the hnRNP C protein.

AB - In the spliceosome, the pre-mRNA, U2 and U6 snRNAs fold into a catalytic structure exhibiting striking similarities with domain V and VI of group II introns. Building of this tripartite structure implies that an evolutionary conserved base pairing between U4 and U6 snRNAs should be disrupted to allow potentially U6 catalytic residue to interact with U2 snRNAs and the pre-mRNA. The steps leading to U4/U6 disruption have been recently discovered and have been shown to involve a modification of the 3' end of U6 snRNA and the hnRNP C protein.

UR - https://linkinghub.elsevier.com/retrieve/pii/030090849684750X

UR - http://www.scopus.com/inward/record.url?scp=0029804708&partnerID=8YFLogxK

U2 - 10.1016/0300-9084(96)84750-X

DO - 10.1016/0300-9084(96)84750-X

M3 - Article

SN - 0300-9084

VL - 78

SP - 436

EP - 442

JO - Biochimie

JF - Biochimie

IS - 6

ER -

Structural features of U6 snRNA and dynamic interactions with other spliceosomal components leading to pre-mRNA splicing

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this