H. G. Wittmann

Austrian Institute of Ecology

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Ada Yonath

Weizmann Institute of Science

Georg Stöffler

Universität Innsbruck

B. Wittmann-Liebold

Max Planck Institute for Molecular Genetics

E. Kaltschmidt

University of Wisconsin–Madison

J. Piefke

Max Planck Institute for Molecular Genetics

J. Müssig

Max Planck Institute for Molecular Genetics

I. Makowski

Max Planck Institute for Molecular Genetics

H.S. Gewitz

Max Planck Institute for Molecular Genetics

Klaus Bartels

Berufsgenossenschaft Rohstoffe und chemische Industrie

I Hindennach

Max Planck Institute for Biology

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Max Planck Society

Max Planck Institute for Molecular Genetics

Weizmann Institute of Science

Max Planck Unit for Structural Molecular Biology

Freie Universität Berlin

Max Planck Institute of Biochemistry

University of Wisconsin–Madison

Centre National de la Recherche Scientifique

University of California, Berkeley

Max Planck Institute for Biology

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Die primäre Proteinstruktur von Stämmen des Tabakmosaikvirus

Zeitschrift für Naturforschung B (1969)

J. Jáuregui-Adell I Hindennach H. G. Wittmann

The sequence of amino acids within the coat protein of the strain Holmes rib grass of tobacco mosaic virus (TMV) has been determined. In this communication the amino acid compositions of the coat protein and of all tryptic peptides are reported. Furthermore the experimental details are given for the elucidation of the amino acid sequences within the first three tryptic peptides, containing 61 amino acids. It has been found that the strain Holmes rib grass differs very extensively in the primary structure from the other TMV strains whose sequences are known. It differs from each of the other strains in more than 50% of the amino acid positions and it contains two amino acids less per protein subunit than the other TMV strains.

Protein primary structure

Strain (injury)

Amino Acid Analysis

10.1515/znb-1969-0715

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Citations (7)

Ribosomal proteins

MGG Molecular & General Genetics (1971)

Georg Stöffler Ellen Deusser H. G. Wittmann David Apirion

Ribosomal protein

Reversion

Independence

10.1007/bf00569785

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Citations (64)

Chemical Structure of Bacterial Ribosomal Proteins

Cold Spring Harbor Monograph Archive (1974)

H. G. Wittmann B. Wittmann-Liebold

INTRODUCTION The isolation of ribosomal proteins which is described in the preceding contribution has enabled chemical, physical and immunological studies to be made on the structure of these proteins. The chemical investigations to be summarized here include studies on the amino acid composition, isoelectric points, N-termini, peptide maps, isolation and analysis of tryptic peptides, and determination of the complete sequence of some proteins. By far the majority of these investigations were done on ribosomal proteins from E. coli and its mutants, but recently similar studies have begun on proteins from Bacillus stearothermophilus ribosomes. Furthermore, conclusions about the chemical structure of ribosomal proteins from numerous bacterial species can be drawn by comparative studies with electrophoretic and immunological methods. ESCHERICHIA COLI WILD TYPE Isoelectric Points It became evident from early electrophoretic studies on E. coli ribosomal proteins (Waller 1964; Leboy, Cox and Flaks 1964) that many of the proteins must be very basic. Determination of the isoelectric point for each of the proteins from E. coli ribosomes was possible by two-dimensional polyacrylamide gel electrophoresis at different pH values (Kaltschmidt 1971). About 70% of the proteins have isoelectric points of pH 10 and higher, whereas those of only three proteins, namely S6, L7 and L12, are at about pH 5. There is no significant difference between 30S and 50S proteins with respect to their isoelectric points. Amino Acid Compositions The basic nature of most E. coli ribosomal proteins is also reflected by their amino acid compositions. However, as it is not possible to...

Ribosomal protein

10.1101/087969110.4.115

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Citations (37)

Correlation of 30S ribosomal proteins ofEscherichia coli isolated in different laboratories

MGG Molecular & General Genetics (1971)

H. G. Wittmann Georg Stöffler I Hindennach C. G. Kurland L. Randall-Hazelbauer

30S

Ribosomal protein

10.1007/bf00569784

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Citations (173)

Lokalisierung von Aminosäureaustauschen bei Nitritmutanten des Tabakmosaikvirus

Molecular Genetics and Genomics (1965)

B. Wittmann-Liebold H. G. Wittmann

Nitrous acid

Glutamic acid

Aspartic acid

Protein primary structure

10.1007/bf02035935

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Citations (19)

Structure and Evolution of Ribosomes

Molecular biology, biochemistry, and biophysics (1980)

H. G. Wittmann

Ribosomal protein

Eukaryotic Ribosome

50S

30S

5.8S ribosomal RNA

5S ribosomal RNA

28S ribosomal RNA

10.1007/978-3-642-81503-4_29

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Citations (11)

Regulation der Protein-Biosynthese

Verhandlungen der Deutschen Gesellschaft für Innere Medizin (1972)

Georg Stöffler H. G. Wittmann

10.1007/978-3-642-85448-4_73

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Citations (1)

Diskussion

VS Verlag für Sozialwissenschaften eBooks (1979)

H. G. Wittmann

10.1007/978-3-663-05355-2_2

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Citations (1)

PROTEIN-RNA INTERACTIONS IN BACTERIAL RIBOSOMES

European Journal of Endocrinology (1973)

R.A. Garrett H. G. Wittmann

ABSTRACT There are several ribosomal proteins which can bind specifically to the three ribosomal RNA's of E. coli . Some structural properties of these proteins and of the RNA are described together with the optimal conditions for binding. Evidence for conformational changes occurring in some proteins, and in the RNA's during binding, is also discussed. The partial localisation of protein binding sites on the 16S and 5S RNA's, and for one protein on the 23S RNA has been attained recently. However, relatively little is known about the regions of the protein which interact with the RNA. Although the nature of the specificity of the protein-RNA interactions is not yet understood, some experimental approaches which are in progress to elucidate the basis of this specificity are mentioned together with a discussion of the structural factors which may be important.

5.8S ribosomal RNA

Ribosomal protein

10.1530/acta.0.074s075

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Citations (3)

Protein Biosynthesis and Its Inhibition by Antibiotics

Springer eBooks (1988)

H. G. Wittmann

Eukaryotic Ribosome

5.8S ribosomal RNA

10.1007/978-3-642-83360-1_1

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Citations (0)