Ionic interactions and the global conformations of the hammerhead ribozyme

G S Bassi; N E Møllegaard; A I Murchie; E von Kitzing; D M Lilley

Ionic interactions and the global conformations of the hammerhead ribozyme

G S Bassi, N E Møllegaard, A I Murchie, E von Kitzing, D M Lilley

Department of Cellular and Molecular Medicine

139 Citations (Scopus)

Abstract

Here we investigate the global conformation of the hammerhead ribozyme. Electrophoretic studies demonstrate that the structure is folded in response to the concentration and type of ions present. Folding based on colinear alignment of arms II and III is suggested, with a variable angle subtended by the remaining helix I. In the probable active conformation, a small angle is subtended between helices I and II. Using uranyl photocleavage, an ion binding site has been detected in the long single-stranded region. The folded conformation could generate a preactivation of the scissile bond to permit in-line attack of the 2'-hydroxyl group, with a bound metal ion playing an integral role in the chemistry.

Original language	English
Journal	Nature Structural and Molecular Biology
Volume	2
Issue number	1
Pages (from-to)	45-55
Number of pages	10
ISSN	1545-9993
Publication status	Published - 1995

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title = "Ionic interactions and the global conformations of the hammerhead ribozyme",

abstract = "Here we investigate the global conformation of the hammerhead ribozyme. Electrophoretic studies demonstrate that the structure is folded in response to the concentration and type of ions present. Folding based on colinear alignment of arms II and III is suggested, with a variable angle subtended by the remaining helix I. In the probable active conformation, a small angle is subtended between helices I and II. Using uranyl photocleavage, an ion binding site has been detected in the long single-stranded region. The folded conformation could generate a preactivation of the scissile bond to permit in-line attack of the 2'-hydroxyl group, with a bound metal ion playing an integral role in the chemistry.",

author = "Bassi, {G S} and M{\o}llegaard, {N E} and Murchie, {A I} and {von Kitzing}, E and Lilley, {D M}",

note = "Keywords: Base Sequence; Binding Sites; Calcium; Consensus Sequence; DNA; Electrophoresis, Polyacrylamide Gel; Magnesium; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Mutagenesis, Site-Directed; Nucleic Acid Conformation; Photolysis; RNA, Catalytic; RNA, Viral; Sodium; Spermine; Uranyl Nitrate; Viroids",

year = "1995",

language = "English",

volume = "2",

pages = "45--55",

journal = "Nature Structural and Molecular Biology",

issn = "1545-9993",

publisher = "nature publishing group",

number = "1",

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TY - JOUR

T1 - Ionic interactions and the global conformations of the hammerhead ribozyme

AU - Bassi, G S

AU - Møllegaard, N E

AU - Murchie, A I

AU - von Kitzing, E

AU - Lilley, D M

N1 - Keywords: Base Sequence; Binding Sites; Calcium; Consensus Sequence; DNA; Electrophoresis, Polyacrylamide Gel; Magnesium; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Mutagenesis, Site-Directed; Nucleic Acid Conformation; Photolysis; RNA, Catalytic; RNA, Viral; Sodium; Spermine; Uranyl Nitrate; Viroids

PY - 1995

Y1 - 1995

N2 - Here we investigate the global conformation of the hammerhead ribozyme. Electrophoretic studies demonstrate that the structure is folded in response to the concentration and type of ions present. Folding based on colinear alignment of arms II and III is suggested, with a variable angle subtended by the remaining helix I. In the probable active conformation, a small angle is subtended between helices I and II. Using uranyl photocleavage, an ion binding site has been detected in the long single-stranded region. The folded conformation could generate a preactivation of the scissile bond to permit in-line attack of the 2'-hydroxyl group, with a bound metal ion playing an integral role in the chemistry.

AB - Here we investigate the global conformation of the hammerhead ribozyme. Electrophoretic studies demonstrate that the structure is folded in response to the concentration and type of ions present. Folding based on colinear alignment of arms II and III is suggested, with a variable angle subtended by the remaining helix I. In the probable active conformation, a small angle is subtended between helices I and II. Using uranyl photocleavage, an ion binding site has been detected in the long single-stranded region. The folded conformation could generate a preactivation of the scissile bond to permit in-line attack of the 2'-hydroxyl group, with a bound metal ion playing an integral role in the chemistry.

M3 - Journal article

C2 - 7719853

SN - 1545-9993

VL - 2

SP - 45

EP - 55

JO - Nature Structural and Molecular Biology

JF - Nature Structural and Molecular Biology

IS - 1

ER -

Ionic interactions and the global conformations of the hammerhead ribozyme

Abstract

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