Protein-RNA interactions in the RNase P holoenzyme from Escherichia coli

Agustín Vioque; John Arnez; Sidney Altman

doi:10.1016/0022-2836(88)90562-1

Protein-RNA interactions in the RNase P holoenzyme from Escherichia coli

Agustín Vioque, John Arnez, Sidney Altman

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

148 Scopus citations

Abstract

The genes for the protein (C5 protein) and RNA (M1 RNA) subunits of Escherichia coli RNase P have been subcloned and their products prepared in milligram quantities by rapid procedures. The interactions between the two subunits of the enzyme have been studied in vitro by a filter-binding technique. The stoichiometry of the subunits in the holoenzyme is 1:1. The dissociation constant for the specific interactions of the subunits in the holoenzyme complex is ~4 × 10^-10 m. C5 protein also interacts with various RNA molecules in a non-specific manner with a dissociation constant of 2 × 10^-8 to 6 × 10^-8 m. Regions of M1 RNA required for interaction with C5 protein have been defined by deletion analysis and footprinting techniques. These interactions are localized primarily between nucleotides 82 to 96 and 170 to 270 of M1 RNA.

Original language	English (US)
Pages (from-to)	835-848
Number of pages	14
Journal	Journal of molecular biology
Volume	202
Issue number	4
DOIs	https://doi.org/10.1016/0022-2836(88)90562-1
State	Published - Aug 20 1988
Externally published	Yes

ASJC Scopus subject areas

Structural Biology
Molecular Biology

Access to Document

10.1016/0022-2836(88)90562-1

Cite this

@article{50b2d993079248f7849b6ecc24d7888b,

title = "Protein-RNA interactions in the RNase P holoenzyme from Escherichia coli",

abstract = "The genes for the protein (C5 protein) and RNA (M1 RNA) subunits of Escherichia coli RNase P have been subcloned and their products prepared in milligram quantities by rapid procedures. The interactions between the two subunits of the enzyme have been studied in vitro by a filter-binding technique. The stoichiometry of the subunits in the holoenzyme is 1:1. The dissociation constant for the specific interactions of the subunits in the holoenzyme complex is ~4 × 10-10 m. C5 protein also interacts with various RNA molecules in a non-specific manner with a dissociation constant of 2 × 10-8 to 6 × 10-8 m. Regions of M1 RNA required for interaction with C5 protein have been defined by deletion analysis and footprinting techniques. These interactions are localized primarily between nucleotides 82 to 96 and 170 to 270 of M1 RNA.",

author = "Agust{\'i}n Vioque and John Arnez and Sidney Altman",

note = "Funding Information: A.V. was a fellow of the Consejo Superior de Investigaciones Cientificas (Spain); this work was started when he was a fellow of the European Molecular Biology Organization. This research was supported by grants to S.A. from the National Institutes of Health and the National Science Foundation of the IJnited States.",

year = "1988",

month = aug,

day = "20",

doi = "10.1016/0022-2836(88)90562-1",

language = "English (US)",

volume = "202",

pages = "835--848",

journal = "Journal of Molecular Biology",

issn = "0022-2836",

publisher = "Academic Press Inc.",

number = "4",

}

TY - JOUR

T1 - Protein-RNA interactions in the RNase P holoenzyme from Escherichia coli

AU - Vioque, Agustín

AU - Arnez, John

AU - Altman, Sidney

N1 - Funding Information: A.V. was a fellow of the Consejo Superior de Investigaciones Cientificas (Spain); this work was started when he was a fellow of the European Molecular Biology Organization. This research was supported by grants to S.A. from the National Institutes of Health and the National Science Foundation of the IJnited States.

PY - 1988/8/20

Y1 - 1988/8/20

N2 - The genes for the protein (C5 protein) and RNA (M1 RNA) subunits of Escherichia coli RNase P have been subcloned and their products prepared in milligram quantities by rapid procedures. The interactions between the two subunits of the enzyme have been studied in vitro by a filter-binding technique. The stoichiometry of the subunits in the holoenzyme is 1:1. The dissociation constant for the specific interactions of the subunits in the holoenzyme complex is ~4 × 10-10 m. C5 protein also interacts with various RNA molecules in a non-specific manner with a dissociation constant of 2 × 10-8 to 6 × 10-8 m. Regions of M1 RNA required for interaction with C5 protein have been defined by deletion analysis and footprinting techniques. These interactions are localized primarily between nucleotides 82 to 96 and 170 to 270 of M1 RNA.

AB - The genes for the protein (C5 protein) and RNA (M1 RNA) subunits of Escherichia coli RNase P have been subcloned and their products prepared in milligram quantities by rapid procedures. The interactions between the two subunits of the enzyme have been studied in vitro by a filter-binding technique. The stoichiometry of the subunits in the holoenzyme is 1:1. The dissociation constant for the specific interactions of the subunits in the holoenzyme complex is ~4 × 10-10 m. C5 protein also interacts with various RNA molecules in a non-specific manner with a dissociation constant of 2 × 10-8 to 6 × 10-8 m. Regions of M1 RNA required for interaction with C5 protein have been defined by deletion analysis and footprinting techniques. These interactions are localized primarily between nucleotides 82 to 96 and 170 to 270 of M1 RNA.

UR - http://www.scopus.com/inward/record.url?scp=0023696278&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023696278&partnerID=8YFLogxK

U2 - 10.1016/0022-2836(88)90562-1

DO - 10.1016/0022-2836(88)90562-1

M3 - Article

C2 - 2459398

AN - SCOPUS:0023696278

VL - 202

SP - 835

EP - 848

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

SN - 0022-2836

IS - 4

ER -

Protein-RNA interactions in the RNase P holoenzyme from Escherichia coli

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this