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10. Gene Expression: Transcription
The McGraw Hill Companies, 2001
Ten
Gene Expression: Transcription
Table 10.5 The Five Small Nuclear Ribonucleoproteins (snRNPs) Involved in
Nuclear Messenger RNA Intron Removal and Their RNAs
snRNP RNA U1 U2 U4 U5 U6 Partial Sequence 3 -UCCAUUCAUA 3 -AUGAUGU 3 -UUGGUCGU . . . AAGGGCACGUAUUCCUU 3 -CAUUUUCCG 3 -CGACUAGU . . . ACA Complementarity 5 end of intron Branch point of intron U6 Exon 1 and exon 2 U2, 5 site Role Recognizes and binds 5 site of intron Binds branch point of intron Binds to (inactivates) U6 Binds to both exons Displaces U1 and binds 5 site and U2 at branch point
Source: With permission from the Annual Review of Genetics, Volume 28 1994 by Annual Reviews www.AnnualReviews.org.
3' HO 15.5 U
5' OH A 16.5
Stem III
15.4 G 15.3 C 15.2 C 15.1 A A 14
C 16.4 G 16.3 G 16.2 U 16.1 C 17
Cleavage site
The hammerhead ribozyme, rst seen in the RNAs of certain viruses (stems I, II, and III). (a) The cleavage point of the substrate (red) is shown using original sequence numbering, relating to the three stems of the hammerheadshaped structure. (b) The cleavage, a transesteri cation, creates a cyclic 2 ,3 -phosphodiester bond and a free 5 -OH.
(Reprinted with permission from Nature, Vol. 372, Heinz W. Pley et al., Three Dimensional Structure of a Hammerhead Ribozyme. Copyright 1994 Macmillan Magazines Limited.)
1.1 1.2 1.3 1.4 1.5 1.6 1.7
L2.4
A 13
L2.3 A L2.2 A
GG C C
11.1 G12
G G U C G C C OH 3'
PPP 5' C C A G C G G 2.1 2.2 2.3 2.4 2.5 2.6 2.7 C3 Stem I U4
C C G G G 10.1A9 L2.1 10.4 G5 G8 Stem II U7 A 6
(a) Cyclic 2',3' phosphodiester bond
O C17 O OH Transesterification OH O G1.1 O OH P O G O P + O
P Free 5' OH (b)
Tamarin: Principles of Genetics, Seventh Edition
III. Molecular Genetics
10. Gene Expression: Transcription
The McGraw Hill Companies, 2001
Eukaryotic DNA Transcription
Exon I 5 GG
Intron A GC
Exon II 3 OH 3 2 4 1 5 CH O 2 O O P O Intron 3 2 G 4 5 CH2 O O P O O OH O 1 O O P O O CH2 O
Lariat G A
Base
Guanine 1
2 4 3
Exon I GC Figure 10.34
Exon II +
Adenine
Self-splicing of a group II intron results in a lariat con guration of the released intron. No external GTP is required since the rst bond transfer takes place with an internal nucleotide, forming the loop of the lariat. A second bond transfer releases the lariat-shaped intron.
presumed pairing is then con rmed. For example, if an A-U base pair occurs between two pieces of RNA, changing the A to a C disrupts the pairing. However, if the U is converted to a G, the pairing is restored (complementary A-U bases are converted to complementary C-G bases via a noncomplementary C-U intermediate). From these techniques, we believe that the following sequence of events takes place. First, the U1 snRNP binds at the 5 site of the intron and the U2 snRNP binds at the branch point ( g. 10.37). The U4, U5, and U6 snRNPs form a single particle. The U4 snRNP releases, freeing the U6 snRNP to bind to the 5 site, displacing the U1 snRNP. (The U1 snRNP, with the help of other proteins, may bind at the 5 site simply to mark it and initiate the process.) The U6 snRNP then also binds the U2 snRNP, allowing the lariat to form in the intron. The U5 snRNP binds the two exon ends together, allowing the splice to be completed as the lariat is removed. The splicing machinery for the majority of introns also includes numerous other polypeptides called auxiliary and splicing factors; the entire splicing process requires about 50 polypeptides. A second, less common, intron, called the U12-dependent intron, with different consensus sequences, also exists. It is removed by a similar splicing process involving different snRNPs (U11, U12) as well as many components shared with the major spliceosome. Currently, we believe the splicing out of the intron may be autocatalyzed, just as in the type II self-splicing introns. The spliceosome may have evolved to ensure control over the process, allowing different introns to splice with differing ef ciencies and allowing alternative splicing to take place. In many eukaryotic genes, alternative paths of splic-
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