TY - JOUR
T1 - Protein folding by domain V of Escherichia coli 23S rRNA
T2 - Specificity of RNA-protein interactions
AU - Samanta, Dibyendu
AU - Mukhopadhyay, Debashis
AU - Chowdhury, Saheli
AU - Ghosh, Jaydip
AU - Pal, Saumen
AU - Basu, Arunima
AU - Bhattacharya, Arpita
AU - Das, Anindita
AU - Das, Debasis
AU - DasGupta, Chanchal
PY - 2008/5
Y1 - 2008/5
N2 - The peptidyl transferase center, present in domain V of 23S rRNA of eubacteria and large rRNA of plants and animals, can act as a general protein folding modulator. Here we show that a few specific nucleotides in Escherichia coli domain V RNA bind to unfolded proteins and, as shown previously, bring the trapped proteins to a folding-competent state before releasing them. These nucleotides are the same for the proteins studied so far: bovine carbonic anhydrase, lactate dehydrogenase, malate dehydrogenase, and chicken egg white lysozyme. The amino acids that interact with these nucleotides are also found to be specific in the two cases tested: bovine carbonic anhydrase and lysozyme. They are either neutral or positively charged and are present in random coils on the surface of the crystal structure of both the proteins. In fact, two of these amino acid-nucleotide pairs are identical in the two cases. How these features might help the process of protein folding is discussed.
AB - The peptidyl transferase center, present in domain V of 23S rRNA of eubacteria and large rRNA of plants and animals, can act as a general protein folding modulator. Here we show that a few specific nucleotides in Escherichia coli domain V RNA bind to unfolded proteins and, as shown previously, bring the trapped proteins to a folding-competent state before releasing them. These nucleotides are the same for the proteins studied so far: bovine carbonic anhydrase, lactate dehydrogenase, malate dehydrogenase, and chicken egg white lysozyme. The amino acids that interact with these nucleotides are also found to be specific in the two cases tested: bovine carbonic anhydrase and lysozyme. They are either neutral or positively charged and are present in random coils on the surface of the crystal structure of both the proteins. In fact, two of these amino acid-nucleotide pairs are identical in the two cases. How these features might help the process of protein folding is discussed.
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U2 - 10.1128/JB.01800-07
DO - 10.1128/JB.01800-07
M3 - Article
C2 - 18310328
AN - SCOPUS:42549084831
SN - 0021-9193
VL - 190
SP - 3344
EP - 3352
JO - Journal of Bacteriology
JF - Journal of Bacteriology
IS - 9
ER -