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The role of proteins and monovalent metal ions in RNP assembly.

Record Type:	Electronic resources : Monograph/item
Title/Author:	The role of proteins and monovalent metal ions in RNP assembly.
Author:	Rambo, Robert Paul.
Description:	231 p.
Notes:	Director: Jennifer A. Doudna.
Notes:	Source: Dissertation Abstracts International, Volume: 64-10, Section: B, page: 4821.
Contained By:	Dissertation Abstracts International64-10B.
Subject:	Biophysics, General.
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3109450
ISBN:	0496569929

The role of proteins and monovalent metal ions in RNP assembly.
Rambo, Robert Paul.

The role of proteins and monovalent metal ions in RNP assembly. [electronic resource] - 231 p.

Director: Jennifer A. Doudna.

Thesis (Ph.D.)--Yale University, 2003.

A structural rationale for the role of monovalent metal ions in the function of large RNA molecules has remained elusive though they are explicitly required for the efficient folding and catalysis of the group I intron, the group II intron and the ribosome. The determination of the X-ray crystal structure of the 160-nucleotide P4--P6 domain from the Tetrahymena thermophila group I intron was a major step towards understanding the folding of large structured RNAs revealing the molecular details of several divalent metal ion binding sites. Using a combination of X-ray diffraction studies and chemical modification experiments on the P4--P6 domain, this work describes a specific monovalent metal ion is integral to the A-A platform of the RNA tetraloop receptor, a common RNA structural motif.

ISBN: 0496569929Subjects--Topical Terms:

226901
Biophysics, General.

The role of proteins and monovalent metal ions in RNP assembly.
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100 0 $a Rambo, Robert Paul. $3 227420
245 1 4 $a The role of proteins and monovalent metal ions in RNP assembly. $h [electronic resource]
300 $a 231 p.
500 $a Director: Jennifer A. Doudna.
500 $a Source: Dissertation Abstracts International, Volume: 64-10, Section: B, page: 4821.
502 $a Thesis (Ph.D.)--Yale University, 2003.
520 # $a A structural rationale for the role of monovalent metal ions in the function of large RNA molecules has remained elusive though they are explicitly required for the efficient folding and catalysis of the group I intron, the group II intron and the ribosome. The determination of the X-ray crystal structure of the 160-nucleotide P4--P6 domain from the Tetrahymena thermophila group I intron was a major step towards understanding the folding of large structured RNAs revealing the molecular details of several divalent metal ion binding sites. Using a combination of X-ray diffraction studies and chemical modification experiments on the P4--P6 domain, this work describes a specific monovalent metal ion is integral to the A-A platform of the RNA tetraloop receptor, a common RNA structural motif.
520 # $a Ribonucleoprotein (RNP) complexes are essential to a wide variety of cellular processes, including protein translocation (SRP), translation (ribosome), genome maintenance (telomerase) and mRNA splicing (spliceosome). A crucial aspect for understanding the function of these complexes will come from a detailed description of how they assemble into active structures. Using the protein-assisted splicing system of the L1.ItrB group II intron and the P4--P6 domain from the Tetrahymena group I intron, this work investigates the requisites of RNP assembly and RNA folding.
520 # $a The L1.ItrB group II intron is an in vitro self-splicing group II intron that encodes a multi-functional protein required for efficient in vivo splicing. Here, I describe the over-expression and complete purification of the L1.ItrB group II intron encoded protein, LtrA. This work demonstrates that the intron-encoded protein recognizes with high affinity two very distinct intronic domains where the equilibrium binding studies make evident a large discrepancy between the empirically determined Kds and the reported kinetically calculated Kds. This discrepancy strongly argues that the native-state of the RNP complex is accomplished by a multi-step induced-fit mechanism. Using a combination of limited-proteolysis and fluorescence spectroscopy, this work establishes that LtrA undergoes a significant RNA-induced structural rearrangement during assembly. This indicates that LtrA itself makes a large contribution to an induced-fit mechanism. It is likely, that this mode of assembly is responsible for the high degree of intron specificity observed for group II intron-encoded proteins for their cognate group II introns.
590 $a School code: 0265.
650 # 0 $a Biophysics, General. $3 226901
650 # 0 $a Chemistry, Biochemistry. $3 226900
710 0 # $a Yale University. $3 212430
773 0 # $g 64-10B. $t Dissertation Abstracts International
790 $a 0265
790 1 0 $a Doudna, Jennifer A., $e advisor
791 $a Ph.D.
792 $a 2003
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