A characterization of the low temperature structural transition of Escherichia coli 5 S RNA by partial enzymatic digestion.

D. Rabin, Teh-hui Kao, D. M. Crothers

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

The low temperature structural transition (low leads to high) of 5 S RNA from Escherichia coli is investigated by partial digestion with ribonuclease T1. In addition to a general masking of guanines from the nuclease, differential changes of accessibility are observed when Mg2+ and salt concentrations are increased to bring about the low leads to high transition. Residue G13 becomes more exposed in the high form while residues G54, G56, G61, G72, and G83-86 become less exposed. The observed cutting rate at other sites is unchanged. A possible conformational change is discussed which could explain the observed changes in RNase T1 digestion patterns as well as the physical chemical observations.

Original languageEnglish (US)
Pages (from-to)10813-10816
Number of pages4
JournalJournal of Biological Chemistry
Volume258
Issue number18
StatePublished - Sep 25 1983

Fingerprint

Ribonuclease T1
Transition Temperature
Escherichia coli
Digestion
RNA
Guanine
Salts
Temperature

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

@article{3bdf4c6db1884dcdb9ce121958fc8d66,
title = "A characterization of the low temperature structural transition of Escherichia coli 5 S RNA by partial enzymatic digestion.",
abstract = "The low temperature structural transition (low leads to high) of 5 S RNA from Escherichia coli is investigated by partial digestion with ribonuclease T1. In addition to a general masking of guanines from the nuclease, differential changes of accessibility are observed when Mg2+ and salt concentrations are increased to bring about the low leads to high transition. Residue G13 becomes more exposed in the high form while residues G54, G56, G61, G72, and G83-86 become less exposed. The observed cutting rate at other sites is unchanged. A possible conformational change is discussed which could explain the observed changes in RNase T1 digestion patterns as well as the physical chemical observations.",
author = "D. Rabin and Teh-hui Kao and Crothers, {D. M.}",
year = "1983",
month = "9",
day = "25",
language = "English (US)",
volume = "258",
pages = "10813--10816",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "18",

}

A characterization of the low temperature structural transition of Escherichia coli 5 S RNA by partial enzymatic digestion. / Rabin, D.; Kao, Teh-hui; Crothers, D. M.

In: Journal of Biological Chemistry, Vol. 258, No. 18, 25.09.1983, p. 10813-10816.

Research output: Contribution to journalArticle

TY - JOUR

T1 - A characterization of the low temperature structural transition of Escherichia coli 5 S RNA by partial enzymatic digestion.

AU - Rabin, D.

AU - Kao, Teh-hui

AU - Crothers, D. M.

PY - 1983/9/25

Y1 - 1983/9/25

N2 - The low temperature structural transition (low leads to high) of 5 S RNA from Escherichia coli is investigated by partial digestion with ribonuclease T1. In addition to a general masking of guanines from the nuclease, differential changes of accessibility are observed when Mg2+ and salt concentrations are increased to bring about the low leads to high transition. Residue G13 becomes more exposed in the high form while residues G54, G56, G61, G72, and G83-86 become less exposed. The observed cutting rate at other sites is unchanged. A possible conformational change is discussed which could explain the observed changes in RNase T1 digestion patterns as well as the physical chemical observations.

AB - The low temperature structural transition (low leads to high) of 5 S RNA from Escherichia coli is investigated by partial digestion with ribonuclease T1. In addition to a general masking of guanines from the nuclease, differential changes of accessibility are observed when Mg2+ and salt concentrations are increased to bring about the low leads to high transition. Residue G13 becomes more exposed in the high form while residues G54, G56, G61, G72, and G83-86 become less exposed. The observed cutting rate at other sites is unchanged. A possible conformational change is discussed which could explain the observed changes in RNase T1 digestion patterns as well as the physical chemical observations.

UR - http://www.scopus.com/inward/record.url?scp=0021112594&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0021112594&partnerID=8YFLogxK

M3 - Article

C2 - 6193117

AN - SCOPUS:0021112594

VL - 258

SP - 10813

EP - 10816

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 18

ER -