An improved method for two-dimensional gel-electrophoresis: Analysis of mutationally altered ribosomal proteins of Escherichia coli

1981 ◽  
Vol 181 (3) ◽  
pp. 309-312 ◽  
Author(s):  
Dieter Geyl ◽  
August Böck ◽  
Katsumi Isono
Keyword(s):  
Escherichia Coli ◽  
Gel Electrophoresis ◽  
Ribosomal Proteins ◽  
Two Dimensional ◽  
Improved Method ◽  
Two Dimensional Gel Electrophoresis

Identification and quantitation of elongation factor EF-P in Escherichia coli cell-free extracts

1980 ◽  
Vol 58 (11) ◽  
pp. 1312-1314 ◽  
Author(s):  
Gynheung An ◽  
Bernard R. Glick ◽  
James D. Friesen ◽  
M. Clelia Ganoza
Keyword(s):  
Escherichia Coli ◽  
Molecular Weight ◽  
Protein Synthesis ◽  
Gel Electrophoresis ◽  
Ribosomal Proteins ◽  
Elongation Factor ◽  
Peptide Bond ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis

EF-P, an elongation factor that stimulates peptide bond synthesis in vitro with some aminoacyl-tRNAs, has been identified by two-dimensional gel electrophoresis and the cellular content at three points in the growth curve has been measured. The molecular weight of EF-P is estimated to be 21 000. EF-P is a slightly acidic protein whose isoelectric point is close to RNA polymerase subunit α. The amount of EF-P present in Escherichia coli is about [Formula: see text]that of EF-G and the level is independent of the stage of cell growth; there is about one EF-P per 10 ribosomes. It is also shown that a highly purified preparation of EF-P is free of all known protein synthesis factors and ribosomal proteins.

Acidic ribosomal proteins of Dictyostelium discoideum that show electrophoretic similarity to Escherichia coli proteins L7 and L12

1989 ◽  
Vol 67 (10) ◽  
pp. 712-718 ◽  
Author(s):  
S. Ramagopal
Keyword(s):  
Escherichia Coli ◽  
Dictyostelium Discoideum ◽  
Gel Electrophoresis ◽  
Ribosomal Proteins ◽  
Sodium Dodecyl ◽  
Slime Mold ◽  
Cellular Slime Mold ◽  
Two Dimensional ◽  
Cellular Slime ◽  
Acidic Proteins

This study documents the presence of three acidic proteins, A1 (pI 4.95), A2 (pI 4.85), and A3 (pI 4.70), in Dictyostelium discoideum ribosomes. All three proteins showed an apparent molecular mass of 13 000 by two-dimensional, sodium dodecyl sulfate gel electrophoresis. They were selectively released by treatment of ribosomes with 50% ethanol – 1 M NH4Cl. The amino acid compositions of A1, A2, and A3 were identical and indicated a predominant amount of alanine. All the above properties are shared by Escherichia coli proteins L7 and L12 and acidic ribosomal proteins in many eukaryotes. Unlike other eukaryotic systems, the acidic proteins of D. discoideum were found associated with the 40S rather than the 60S ribosomal subunit. Acidic proteins analogous in size and electrophoretic mobility to those of D. discoideum were also detected in several other cellular slime mold strains. Not one of the cellular slime mold acidic proteins reacted with antibodies to E. coli proteins L7 and L12 in immunodiffusion tests. In D. discoideum, the distribution of acidic proteins was altered during development. Amoebae contained all three proteins. In spores, A, was absent and the relative amounts of A2 and A3 were lower than in amoebae. In addition, nine other acidic ribosomal proteins exhibited differences between vegetative amoebae and spores.Key words: acidic ribosomal proteins, development, cellular slime mold, L7 and L12 proteins, two-dimensional gel electrophoresis.

Analysis of Ribosomal Proteins from a Yellow Mutant of Chlamydomonas reinhardii by Two-dimensional Gel Electrophoresis

1979 ◽  
Vol 174 (9) ◽  
pp. 822-830 ◽  
Author(s):  
István Gyurján ◽  
Géza Erdös ◽  
Nadiezda P. Yurina ◽  
Marina S. Turischeva ◽  
Margarita S. Odintsova
Keyword(s):  
Gel Electrophoresis ◽  
Ribosomal Proteins ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Chlamydomonas Reinhardii

scholarly journals Reductive alkylation of ribosomes as a probe to the topography of ribosomal proteins*

1974 ◽  
Vol 143 (3) ◽  
pp. 607-612 ◽  
Author(s):  
Graham Moore ◽  
Robert R. Crichton
Keyword(s):  
Escherichia Coli ◽  
Protein Complex ◽  
Gel Electrophoresis ◽  
Ribosomal Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Two Dimensional ◽  
Reductive Alkylation ◽  
Lysine Residues

Escherichia coli ribosomes were treated with a number of different aldehydes of various sizes in the presence of NaBH4. After incorporation of either 3H or 14C, the ribosomal proteins were separated by two-dimensional polyacrylamide-gel electrophoresis and the extent of alkylation of the lysine residues in each protein was measured. The same pattern of alkylation was observed with the four reagents used, namely formaldehyde, acetone, benzaldehyde and 3,4,5-trimethoxybenzaldehyde. Every protein in 30S and 50S subunits was modified, although there was considerable variation in the degree of alkylation of individual proteins. A topographical classification of ribosomal proteins is presented, based on the degree of exposure of lysine residues. The data indicate that every protein of the ribosome has at least one lysine residue exposed at or near the surface of the ribonucleo-protein complex.

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