Molecular mechanism of in vitro 30 S ribosome assembly. II. Conformational changes of ribosomal proteins.

Jm, Dunn; Kp, Wong

doi:10.1016/s0021-9258(18)36004-6

Journal of Biological Chemistry

1979

DOI: 10.1016/s0021-9258(18)36004-6

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Molecular mechanism of in vitro 30 S ribosome assembly. II. Conformational changes of ribosomal proteins.

Dunn Jm¹,

Wong Kp²

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1979

1986

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Cited by 4 publications

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“…Furthermore, the recent demonstrations that the constituent proteins and RNA do possess unique three-dimensional structures under the conditions of reconstitution (Allen & Wong, 1978a-c, 1979; Luer & Wong, 1979) suggest that the self-assembly probably proceeds by specific molecular recognitions of the protein and RNA components during their interactions to form the 30S ribosomal subunit. These interactions also involve the complex conformational changes of the 16S RNA (Hochkeppel & Craven, 1977; Dunn & Wong, 1979a) and those of the proteins (Dunn & Wong, 1979b) and the resulting reconstituted intermediates (RI and RI*) (Dunn & Wong, 1979c).…”

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Conformational stability of ribosomal protein L7/L12: effects of pH, temperature, and guanidinium chloride

Luer¹,

Wong²

1980

Biochemistry

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The effects of pH, temperature, and guanidinium chloride on the conformation of ribosomal protein L7/L12 have been investigated in order to understand the stability of this protein dimer. The results indicate that many of the molecular forces stabilizing the conformation of the dimer are disrupted at low pH or high temperature. These acid- and thermal-denatured states, however, still retain considerable secondary structure. Approximately half of the alpha-helical content present in the native protein remains intact at pH below 2 and at temperatures above 90 degrees C. Further denaturation of the acid-denatured protein by 6 M guanidinium chloride results in a state which still contains approximately 20% alpha helix. Similar amounts of residual conformation remain when the native L7/L12 dimer is denatured with guanidinium chloride. Thermodynamic analysis of the conformational transitions studied indicates that none is compatible with a simple two-state process. The complexity of these denaturation data and the structural characterizations of the various denatured states are consistent with the possible existence of structural domains in the protein molecule possessing different conformational stabilities.

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Conformational stability of ribosomal protein L7/L12: effects of pH, temperature, and guanidinium chloride

Luer¹,

Wong²

1980

Biochemistry

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The role of magnesium and potassium ions in the molecular mechanism of ribosome assembly: Hydrodynamic, conformational, and thermal stability studies of 16 S RNA from Escherichia coli ribosomes

Allen¹,

Wong²

1986

Archives of Biochemistry and Biophysics

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Molecular mechanism of in vitro 30 S ribosome assembly. I. Conformational changes of the 16 S RNA.

Dunn¹,

Wong²

1979

Journal of Biological Chemistry

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Molecular mechanism of in vitro 30 S ribosome assembly. II. Conformational changes of ribosomal proteins.

Cited by 4 publications

References 34 publications

Conformational stability of ribosomal protein L7/L12: effects of pH, temperature, and guanidinium chloride

Conformational stability of ribosomal protein L7/L12: effects of pH, temperature, and guanidinium chloride

The role of magnesium and potassium ions in the molecular mechanism of ribosome assembly: Hydrodynamic, conformational, and thermal stability studies of 16 S RNA from Escherichia coli ribosomes

Molecular mechanism of in vitro 30 S ribosome assembly. I. Conformational changes of the 16 S RNA.

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