Functions of the Abundant U-snRNPs
Functions of the Abundant U-snRNPs
复制标题
丰富的 U-snRNP 的功能
DOI:
10.1007/978-3-642-73020-7_5
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发表时间:
1988
影响因子:
3.7
通讯作者:
W. Keller
中科院分区:
文献类型:
--
作者:
J. Steitz;D. Black;V. Gerke;K. A. Parker;A. Krämer;D. Frendewey;W. Keller
In this chapter experiments are reviewed which led from the initial hypothesis about the role of U1 snRNP in pre-mRNA splicing to the elucidation of the function of all abundant nucleoplasmic snRNPs (Ul, U2, U4/6, and U5) in higher eukaryotes. As discussed also by others (Lustig et al. 1986; Padgett et al. 1986; Green 1986; Maniatis and Reed 1987; Sharp 1987), the events leading from the synthesis of the primary transcript to the spliced product can be divided into distinct steps: there must exist mechanisms by which the distant splice sites are recognized, brought into proximity, and precisely aligned. This is a prerequisite for the actual chemical cleavage-ligation reactions which result in intron excision and exon ligation. In the case of the self-splicing RNAs the recognition alignment is accomplished by specific intramolecular base pairing interactions (cis-alignment) and the cleavage ligation is mediated by catalytic RNA sequences located within the intron (reviewed by Cech and Bass 1986). In contrast, nuclear pre- mRNA splicing, as studied in vitro, requires a multitude of transacting components. Recognition takes place by the specific binding of snRNPs to conserved pre-mRNA sequences. The U1 snRNP interacts with the 5’ splice site, the U2 snRNP with the branch site, and the U5 snRNP most likely with the 3’ splice site. There is compelling evidence that the mode of recognition of U1 snRNP operates via intermolecular base pairing between sequences at the 5’ end of the U1 snRNA and sequences at the 5’ splice sites of pre-mRNAs. Likewise it has been shown in S. cerevisiae that its U2 analog (LSR1 or snR20) recognizes the conserved branchpoint consensus via base pairing to an internal snRNA sequence. In contrast, the binding of U5 snRNP appears to be mediated by a specific protein which is able to recognize the polypyrimidine tract located immediately upstream of the 3’ splice sites. The U4/U6 particle, although participating in splicing, may not bind directly to pre-mRNA but may instead interact with the other snRNPs to fold the splicing complex into a specific spatial configuration which results in the precise alignment of the splice sites. The ordered and sequential binding of the major U- snRNPs to the pre-mRNA is mediated by additional protein factors and leads to the stepwise assembly of large multicomponent complexes called spliceosomes, the formation of which can be studied by sedimentation in velocity gradients or by electrophoresis in nondenaturing acrylamide gels.
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影响因子:
10.5
作者:
LIN, RJ;LUSTIG, AJ;ABELSON, J
通讯作者:
ABELSON, J
DOI:
--
发表时间:
1983
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Hinterberger,M;Pettersson,I;Steitz,JA
通讯作者:
Steitz,JA
DOI:
10.1073/pnas.83.4.887
发表时间:
1986
影响因子:
11.1
作者:
Perkins,KK;Furneaux,HM;Hurwitz,J
通讯作者:
Hurwitz,J
DOI:
10.1002/j.1460-2075.1986.tb04412.x
发表时间:
1986
期刊:
The EMBO journal
影响因子:
--
作者:
Vijayraghavan,U;Parker,R;Tamm,J;Iimura,Y;Rossi,J;Abelson,J;Guthrie,C
通讯作者:
Guthrie,C
DOI:
--
发表时间:
1985
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Lischwe,MA;Ochs,RL;Reddy,R;Cook,RG;Yeoman,LC;Tan,EM;Reichlin,M;Busch,H
通讯作者:
Busch,H