Catalysis by the RNA subunit of RNase P - a minireview

S. Altman; M. F. Baer; M. Bartkiewicz; H. Gold; C. Guerrier-Takada; L. A. Kirsebom; N. Lumelsky; K. Peck

doi:10.1016/0378-1119(89)90030-9

Catalysis by the RNA subunit of RNase P - a minireview

S. Altman, M. F. Baer, M. Bartkiewicz, H. Gold, C. Guerrier-Takada, L. A. Kirsebom, N. Lumelsky, K. Peck

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

35 Scopus citations

Abstract

RNase P, an enzyme that contains both RNA and protein components, cleaves tRNA precursors to generate mature 5′ termini. The catalytic activity of RNase P resides in the RNA component, with the protein cofactor affecting the rate of the cleavage reaction. The reaction is also influenced by the nature of the tRNA substrate.

Original language	English (US)
Pages (from-to)	63-64
Number of pages	2
Journal	Gene
Volume	82
Issue number	1
DOIs	https://doi.org/10.1016/0378-1119(89)90030-9
State	Published - Oct 15 1989
Externally published	Yes

Keywords

Catalytic RNA
M1 RNA structure and function
model substrates
nucleotide sequences
protein cofactor

ASJC Scopus subject areas

Genetics

Access to Document

10.1016/0378-1119(89)90030-9

Cite this

@article{60808250d6c94b99bb753b1d8ee7f009,

title = "Catalysis by the RNA subunit of RNase P - a minireview",

abstract = "RNase P, an enzyme that contains both RNA and protein components, cleaves tRNA precursors to generate mature 5′ termini. The catalytic activity of RNase P resides in the RNA component, with the protein cofactor affecting the rate of the cleavage reaction. The reaction is also influenced by the nature of the tRNA substrate.",

keywords = "Catalytic RNA, M1 RNA structure and function, model substrates, nucleotide sequences, protein cofactor",

author = "S. Altman and Baer, {M. F.} and M. Bartkiewicz and H. Gold and C. Guerrier-Takada and Kirsebom, {L. A.} and N. Lumelsky and K. Peck",

note = "Funding Information: Work in the laboratoryo f S.A. is supportedb y grantsf rom the USPHS and USNSF. K.P. is the recipiento f a predoctoratlr aininga ward.N .L. is the recipient of a postdoctoralf ellowship from the USPHS.",

year = "1989",

month = oct,

day = "15",

doi = "10.1016/0378-1119(89)90030-9",

language = "English (US)",

volume = "82",

pages = "63--64",

journal = "Gene",

issn = "0378-1119",

publisher = "Elsevier",

number = "1",

}

TY - JOUR

T1 - Catalysis by the RNA subunit of RNase P - a minireview

AU - Altman, S.

AU - Baer, M. F.

AU - Bartkiewicz, M.

AU - Gold, H.

AU - Guerrier-Takada, C.

AU - Kirsebom, L. A.

AU - Lumelsky, N.

AU - Peck, K.

N1 - Funding Information: Work in the laboratoryo f S.A. is supportedb y grantsf rom the USPHS and USNSF. K.P. is the recipiento f a predoctoratlr aininga ward.N .L. is the recipient of a postdoctoralf ellowship from the USPHS.

PY - 1989/10/15

Y1 - 1989/10/15

N2 - RNase P, an enzyme that contains both RNA and protein components, cleaves tRNA precursors to generate mature 5′ termini. The catalytic activity of RNase P resides in the RNA component, with the protein cofactor affecting the rate of the cleavage reaction. The reaction is also influenced by the nature of the tRNA substrate.

AB - RNase P, an enzyme that contains both RNA and protein components, cleaves tRNA precursors to generate mature 5′ termini. The catalytic activity of RNase P resides in the RNA component, with the protein cofactor affecting the rate of the cleavage reaction. The reaction is also influenced by the nature of the tRNA substrate.

KW - Catalytic RNA

KW - M1 RNA structure and function

KW - model substrates

KW - nucleotide sequences

KW - protein cofactor

UR - http://www.scopus.com/inward/record.url?scp=0024446858&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0024446858&partnerID=8YFLogxK

U2 - 10.1016/0378-1119(89)90030-9

DO - 10.1016/0378-1119(89)90030-9

M3 - Article

C2 - 2479591

AN - SCOPUS:0024446858

SN - 0378-1119

VL - 82

SP - 63

EP - 64

JO - Gene

JF - Gene

IS - 1

ER -

Catalysis by the RNA subunit of RNase P - a minireview

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this