Brigitte Wittmann‐Liebold

Wita Proteomics (Germany)

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Albrecht Otto

Max Delbrück Center

Volker Kruft

PerkinElmer (Germany)

Bernd Thiede

University of Oslo

Henning Urlaub

Max Planck Institute for Multidisciplinary Sciences

Johann Salnikow

Technische Universität Berlin

Eva‐Christina Müller

Humboldt-Universität zu Berlin

Hanns‐Rüdiger Graack

Wita Proteomics (Germany)

Roza Maria Kamp

Berliner Hochschule für Technik

Peter R. Jungblut

Max Planck Institute for Infection Biology

Keith Ashman

TissuPath

Cooperative Institutions

Max Planck Institute for Molecular Genetics

Max Planck Society

Max Delbrück Center

Freie Universität Berlin

Charité - Universitätsmedizin Berlin

Centre National de la Recherche Scientifique

Humboldt-Universität zu Berlin

National Institutes of Health

Baylor College of Medicine

Heidelberg University

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The primary structure of ribosomal protein S7 from E. Coli strains K and B

FEBS Letters (1978)

Joseph Reinbolt Denis Tritsch Brigitte Wittmann‐Liebold

Resume Les proteines ribosomiques S7 de la sousunite 30S d'Escherichia coli des souches K et B different sensiblement par leur composition en acides amines. Nous presentons en detail la determination de la structure primaire des proteines S7K et S7B. La proteine S7K est constituee de 177 acides amines correspondant a un poids moleculaire de 19 732, alors que la proteine S7B ne renferme que 153 acides amines pour un poids moleculaire de 17 131, soit une difference de 24 acides amines. La sequence de ces proteines a ete etablie partiellement au moyen d'un sequenceur automatique Beckman modifie. De plus amples informations ont ete obtenues par l'isolement et l'etude de differents peptides soit trypsiques, soit thermolysiques, soit pepsiques, ou encore de ceux resultant de la digestion par la protease de Staphylococcus aureus. Enfin, l'alignement de tous ces peptides a pu etre obtenu sans ambiguite par l'etude de grands peptides de recouvrement obtenus par coupure au moyen de reactifs chimiques soit au niveau de liaisons tryptophanyl (par le 2-(2-nitrophenylesulphenile)-3-methyle-3′ bromoindolenine), soit au niveau des liaisons methionyl (par le bromure de cyanogene). Nous avons aussi caracterise la nature de la mutation conduisant aux differentes proteines S7B et S7K. Il apparait que S7K presente une elongation de 24 acides amines a sa partie C-terminale. La sequence des proteines S7K et S7B a ete comparee a celle d'autres proteines ribosomiques en vue d'etablir des homologies. Enfin nous avons calcule la structure secondaire la plus probable pour ces deux proteines.

10.1016/0014-5793(78)81196-x

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Citations (38)

An Embryonic Inducing Factor: Isolation by High Performance Liquid Chromatography and Chemical Properties

Biological Chemistry Hoppe-Seyler (1985)

Jan Born P. Höppe Walter Schwarz Hildegard Tiedemann Heinz Tiedemann

A protein (vegetalizing factor) which induces amphibian gastrula ectoderm to tissues which in normal development are derived from endoderm and mesoderm has been isolated from chicken embryo trunks by a combination of size exclusion and reversed phase HPLC. An amount of 0.5 ng factor per gastrula evokes inductions in 80-100% of the cases. The protein (apparent Mr approximately 13 000) is split by NaBH4 to polypeptide chains of about half the size under conditions in which disulfide bridges are reduced. The biological activity is lost.

10.1515/bchm3.1985.366.2.729

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Citations (20)

The number of copies of ribosome-bound proteins L7 and L12 required for protein synthesis activity.

Journal of Biological Chemistry (1981)

C.C. Lee C R Cantor Brigitte Wittmann‐Liebold

Poly(U)-dependent poly(Phe) synthesis and elongation factor G (EF-G)-dependent GTPase activity were used to study the partial reconstitution of L7/L12-deficient ribosomes with proteins L7/L12 and fluorescent conjugates.Seventy-five per cent of these activities are restored when unmodified L7/L12 dimer is added to L7/L12-deficient cores at a ratio of 1:l.Various covalent fluorescent conjugates of L7/L12 bind to these cores about as well as unmoidifed protein.A fluorescein-5-isothiocyanate derivative of L12 shows almost no functional activity when bound.However, mixed reconstitutes of this conjugate and unmodified L12 have 75% functional activity when half the protein is unmodified.These results can be explained by a model in which there are two independent binding sites on the ribosome for two dimers of L7/L12.The binding of dimers to ribosomes is totally random and complete; the particle is 100% active so long as it has one active dimer bound to either one of the two sites.However, more complex models cannot be ruled out.An 5-(io-doacetamidoethy1)-aminonaphthalene-1-sulfonic acid (IAEDANS) derivative of L7 is labeled semispecifically at the COOH terminus.This conjugate shows partial functional activity.When assay results are analyzed using the above model, it appears that the specific COOH-terminal modification has no effect on activity.However, all but a small fraction of the nonspecific IAEDANS modifications lead to inactivation.Ribosomal proteins L7 and L12l are identical except for the NH2-terminal serine which is acetylated in L7 (1).L7/L12 is the only protein present in multiple copies on the 70 S Escherichia coli ribosome (2).Recent studies show that the number of copies is likely to be four monomers or two dimers (3-5).Extensive studies by several groups indicate a key role for L7/L12 in the proper interactions of ribosomes with initiation, elongation, and termination factors (6).Protein L7/L12 can be specifically removed from 70 S ribosomes or 50 S subunits (7).The L7/LlB-deficient core particles are incapable of synthesizing polypeptide chains.L7/L12 can be rebound to these particles and the resulting partially reconstituted ribo-

10.1016/s0021-9258(19)70094-5

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Citations (26)

Identification of apoptosis-associated proteins in a human Burkitt lymphoma cell line. Cleavage of heterogeneous nuclear ribonucleoprotein A1 by caspase 3.

Journal of Biological Chemistry (1998)

Ekkehard Brockstedt Anke Rickers Susanne Kostka Andreas Laubersheimer Bernd Dörken

Page 28060, Fig. 2: The numbering of the altered protein spots should be as follows. B1-3 should read D1-3; B4-6 must be D4-6; I must be F; J must be G; B′3-4 must be D′3-4; and B′1-2 must read D′1-2. The spots A1-6 and A7 have to be deleted in the figure. The new Fig. 2 is shown below:

Cleavage (geology)

Heterogeneous nuclear ribonucleoprotein

10.1016/s0021-9258(19)88612-x

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Citations (10)

Cartography of Ribosomal Proteins of the 30S Subunit from the Halophilic Haloarcula Marismortui and Complete Sequence Analysis of Protein HS26

European Journal of Biochemistry (1995)

Sabine Engemann Ruth Noelle Eike Herfurth Ulrike Briesemeister Gerlinde Grelle

By two-dimensional polyacrylamide gel electrophoresis of 30S ribosomal subunit proteins (S proteins) from Haloarcula marismortui we identified 27 distinct spots and analyzed all of them by protein sequence analysis. We demonstrated that protein HmaS2 (HS2) is encoded by the open reading frame orfMSG and has sequence similarities to the S2 ribosomal protein family. The proteins HmaS5 and HmaS14 were identified as spots HS7 and HS21/HS22, respectively. Protein HS4 was characterized by amino-terminal sequence analysis. The spot HS25 was recognized as an individual protein and also characterized by sequence analysis. Furthermore, the complete primary sequence of HS26 is reported, showing similarity only to eukaryotic ribosomal proteins. The sequence data of a further basic protein shows a high degree of similarity to ribosomal protein S12, therefore, it was designated HmaS12. Slightly different results compared to published sequence data were obtained for the protein HS12 and HmaS19. The putative 'ribosomal' protein HSH could not be localized in the two-dimensional pattern of the total 30S ribosomal subunit proteins of H. marismortui. Therefore, it seems to be unlikely that this protein is a real constituent of the H. marismortui ribosome.

Ribosomal protein

30S

Eukaryotic Ribosome

Sequence (biology)

10.1111/j.1432-1033.1995.024_c.x

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Citations (3)

Analysis of demethylaminoazobenzene-thiohydantoins of amino acid by high-pressure liquid chromatography

Analytical Biochemistry (1980)

Jia‐Yaw Chang Arnold Lehmann Brigitte Wittmann‐Liebold

Isoleucine

Phenyl isothiocyanate

Amino Acid Analysis

10.1016/0003-2697(80)90171-2

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Citations (35)

The primary structure of Bacillus subtilis acidic ribonsomal protein B-19. Isolation and characterization of peptides and the complete amino acid sequence.

PubMed (1980)

Takuzì Itoh Brigitte Wittmann‐Liebold

The complete primary structure of Bacillus subtilis acidic protein B-L9, functionally equivalent to protein L7/L12 from E. coli, has been determined. B-L9 is composed of 122 residues and has the amino acid composition: Asp3, ASN3, Thr4, Ser3, Glu22, Gln1, Pro3, Gly11, Ala21, Val14, Ile9, Leu12, Phe2, Lys13, and Arg1. The molecular weight of B-L9 is 12,633. The amino acid sequence was determined by a combination of automated Edman degradation of the intact protein in a modified Beckman sequenator, and micro dansyl-Edman degradation of the peptides obtained from digestions with trypsin, thermolysin, Staphylococcus aureus protease, chymotrypsin and pepsin. A comparison of protein B-L9 from B. subtilis with E-L12 from E. coli shows a relatively high degree of homology.

Thermolysin

Edman degradation

Protein primary structure

Pepsin

Source

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Citations (12)

The Translational Apparatus

Springer eBooks (1993)

Knud H. Nierhaus F. Franceschi Alap R. Subramanian Volker A. Erdmann Brigitte Wittmann‐Liebold

10.1007/978-1-4615-2407-6

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Citations (192)

The primary structure of protein S14 from the small ribosomal subunit of Escherichia coli

FEBS Letters (1983)

Makoto Yaguchi C. Roy Reinhart A.F. Reithmeier Brigitte Wittmann‐Liebold H. G. Wittmann

Protein S14 was isolated in pure form from Escherichia coli ribosomal 30 S subunits. Its complete amino acid sequence was determined by a combination of various approaches, such as enzymatic and chemical cleavage of the protein chain, isolation of the resulting peptides as well as manual and automatic sequence determination by the Edman degradation technique. The protein has an M r of 11 191 and consists of 98 amino acid residues, 26 of which are basic and 9 acidic. One residue each of cysteine, histidine, tyrosine and tryptophan is present in the protein. The secondary structure of protein S14 as predicted according to 4 different programs shows a long α‐helix in the N‐terminal region and a short α‐helix near the C‐terminus of the protein chain. When the amino acid sequence of protein S14 was compared with that of all other E. coli ribosomal proteins with computer search programs, only relatively short homologous regions were found. A comparison between protein S14 of E. coli and the homologous protein from Bacillus stearothermophilus revealed ∼35% identity within the protein regions available for comparison.

Ribosomal protein

Edman degradation

Protein primary structure

Protein sequencing

10.1016/0014-5793(83)80869-2

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Citations (15)

Mitochondrial ribosomal proteins (MRPs) of yeast

Biochemical Journal (1998)

Hanns‐Rüdiger Graack Brigitte Wittmann‐Liebold

Mitochondrial ribosomal proteins (MRPs) are the counterparts in that organelle of the cytoplasmic ribosomal proteins in the host. Although the MRPs fulfil similar functions in protein biosynthesis, they are distinct in number, features and primary structures from the latter. Most progress in the eludication of the properties of individual MRPs, and in the characterization of the corresponding genes, has been made in baker's yeast (Saccharomyces cerevisiae). To date, 50 different MRPs have been determined, although biochemical data and mutational analysis propose a total number which is substantially higher. Surprisingly, only a minority of the MRPs that have been characterized show significant sequence similarities to known ribosomal proteins from other sources, thus limiting the deduction of their functions by simple comparison of amino acid sequences. Further, individual MRPs have been characterized functionally by mutational studies, and the regulation of expression of MRP genes has been described. The interaction of the mitochondrial ribosomes with transcription factors specific for individual mitochondrial mRNAs, and the communication between mitochondria and the nucleus for the co-ordinated expression of ribosomal constituents, are other aspects of current MRP research. Although the mitochondrial translational system is still far from being described completely, the yeast MRP system serves as a model for other organisms, including that of humans.

Ribosomal protein

Mitochondrial ribosome

Organelle

10.1042/bj3290433

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Citations (128)