Metal ions and ribosomal conformation

Moshe Tal

doi:10.1016/0005-2787(69)90604-2

Metal ions and ribosomal conformation

Moshe Tal

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

40 Scopus citations

Abstract

Divalent metal ions play an important role in preserving the compact structure of ribosomes. This is reflected in the specific viscosity (η_sp) of the ribosomal solution which is increased at elevated temperatures in the presence of EDTA. Dialysis of EDTA-treated ribosomes (unfolded particles) against 1 mM Zn²⁺, Ni²⁺, Mn²⁺, Co²⁺ and Fe²⁺ (present in natural ribosomes) results in a sedimentation profile closely similar to that of natural ribosomes, indicating reversibility of the unfolding process caused by EDTA. On the other hand, addition of Mg²⁺ to the unfolded particles results in intermediate s values only. An extended thermal denaturation scheme of ribosomes, taking into consideration the role of metal ions, is proposed.

Original language	English
Pages (from-to)	76-86
Number of pages	11
Journal	BBA Section Nucleic Acids And Protein Synthesis
Volume	195
Issue number	1
DOIs	https://doi.org/10.1016/0005-2787(69)90604-2
State	Published - 19 Nov 1969
Externally published	Yes

ASJC Scopus subject areas

General Medicine

Access to Document

10.1016/0005-2787(69)90604-2

Cite this

@article{5eaaada463b34e3f8bd06a087a0ca324,

title = "Metal ions and ribosomal conformation",

abstract = "Divalent metal ions play an important role in preserving the compact structure of ribosomes. This is reflected in the specific viscosity (ηsp) of the ribosomal solution which is increased at elevated temperatures in the presence of EDTA. Dialysis of EDTA-treated ribosomes (unfolded particles) against 1 mM Zn2+, Ni2+, Mn2+, Co2+ and Fe2+ (present in natural ribosomes) results in a sedimentation profile closely similar to that of natural ribosomes, indicating reversibility of the unfolding process caused by EDTA. On the other hand, addition of Mg2+ to the unfolded particles results in intermediate s values only. An extended thermal denaturation scheme of ribosomes, taking into consideration the role of metal ions, is proposed.",

author = "Moshe Tal",

year = "1969",

month = nov,

day = "19",

doi = "10.1016/0005-2787(69)90604-2",

language = "English",

volume = "195",

pages = "76--86",

journal = "BBA Section Nucleic Acids And Protein Synthesis",

issn = "0005-2787",

publisher = "Elsevier B.V.",

number = "1",

}

TY - JOUR

T1 - Metal ions and ribosomal conformation

AU - Tal, Moshe

PY - 1969/11/19

Y1 - 1969/11/19

N2 - Divalent metal ions play an important role in preserving the compact structure of ribosomes. This is reflected in the specific viscosity (ηsp) of the ribosomal solution which is increased at elevated temperatures in the presence of EDTA. Dialysis of EDTA-treated ribosomes (unfolded particles) against 1 mM Zn2+, Ni2+, Mn2+, Co2+ and Fe2+ (present in natural ribosomes) results in a sedimentation profile closely similar to that of natural ribosomes, indicating reversibility of the unfolding process caused by EDTA. On the other hand, addition of Mg2+ to the unfolded particles results in intermediate s values only. An extended thermal denaturation scheme of ribosomes, taking into consideration the role of metal ions, is proposed.

AB - Divalent metal ions play an important role in preserving the compact structure of ribosomes. This is reflected in the specific viscosity (ηsp) of the ribosomal solution which is increased at elevated temperatures in the presence of EDTA. Dialysis of EDTA-treated ribosomes (unfolded particles) against 1 mM Zn2+, Ni2+, Mn2+, Co2+ and Fe2+ (present in natural ribosomes) results in a sedimentation profile closely similar to that of natural ribosomes, indicating reversibility of the unfolding process caused by EDTA. On the other hand, addition of Mg2+ to the unfolded particles results in intermediate s values only. An extended thermal denaturation scheme of ribosomes, taking into consideration the role of metal ions, is proposed.

UR - http://www.scopus.com/inward/record.url?scp=0014684430&partnerID=8YFLogxK

U2 - 10.1016/0005-2787(69)90604-2

DO - 10.1016/0005-2787(69)90604-2

M3 - Article

AN - SCOPUS:0014684430

SN - 0005-2787

VL - 195

SP - 76

EP - 86

JO - BBA Section Nucleic Acids And Protein Synthesis

JF - BBA Section Nucleic Acids And Protein Synthesis

IS - 1

ER -

Metal ions and ribosomal conformation

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this