Isolation and characterization of a new ribosomal protein from the thermophilic eubacteria, Thermus thermophilus, T. aquaticus and T. flavus.
A ribosomal protein, showing no homology with other known prokaryotic ribosomal proteins, was isolated and characterized from the thermophilic eubacteria, Thermus thermophilus, T. aquaticus and T. flavus. This small (26 amino acids) and strongly basic (1 acidic and 13 basic residues) protein displayed the same primary structure from all three sources. Interestingly, it shows about 65% homology with a ribosomal protein from spinach chloroplasts (J. Schmidt, personal communication).
Choli
T
T
School of Chemistry, Laboratory of Biochemistry, Aristotle University of Thessaloniki, Greece.
Franceschi
F
F
Yonath
A
A
Wittmann-Liebold
B
B
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification*; D002851:Chromatography, High Pressure Liquid; D015180:Electrophoresis, Gel, Two-Dimensional; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D012269:Ribosomal Proteins / Q000737:chemistry / Q000302:isolation & purification*; D017386:Sequence Homology, Amino Acid; D013824:Thermus / Q000737:chemistry*; D016963:Thermus thermophilus / Q000737:chemistry*
D001426:Bacterial Proteins; D012269:Ribosomal Proteins; C082829:Thx protein, Thermus