[RNA-binding properties of ribosomal protein L1 from Thermus thermophilus].
Fragments of the ribosomal protein L1 from Thermus thermophilus were obtained by limited trypsinolysis and spontaneous proteolysis. Binding of the intact L1 and its proteolytic fragments to 23S ribosomal RNA was studied. First eight N-terminal amino acids are important for RNA binding because protein L1 lacking these amino acids exhibits reduced 23S rRNA binding. Additional cleavage of the polypeptide chain between residues 36 and 37 completely abolishes RNA binding. Comparison of these data with recently determined structure of protein L1 from T. thermophilus suggests the nature of interactions which can determine specific and strong association of the protein L1 with 23S rRNA.
Elisekina
I A
IA
Avliiakulov
N K
NK
Grishkovskaia
I B
IB
Muranova
T A
TA
Sedel'nikova
S E
SE
Garber
M B
MB
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000378:metabolism*; D008969:Molecular Sequence Data; D012329:RNA, Bacterial / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000378:metabolism*; D012269:Ribosomal Proteins / Q000378:metabolism*; D016963:Thermus thermophilus / Q000378:metabolism*
D001426:Bacterial Proteins; D012329:RNA, Bacterial; D016601:RNA-Binding Proteins; D012269:Ribosomal Proteins; C028546:ribosomal protein L1