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Affinity of ribosomal protein S8 from mesophilic and (hyper)thermophilic archaea and bacteria for 16S rRNA correlates with the growth temperatures of the organisms
Author(s) -
Gruber Thomas,
Köhrer Caroline,
Lung Birgit,
Shcherbakov Dmitri,
Piendl Wolfgang
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)00760-9
Subject(s) - thermophile , thermus thermophilus , hyperthermophile , thermostability , ribosomal protein , archaea , ribosomal rna , biology , ribosome , thermus , bacteria , biochemistry , mesophile , escherichia coli , 16s ribosomal rna , microbiology and biotechnology , rna , genetics , enzyme , gene
The ribosomal protein S8 plays a pivotal role in the assembly of the 30S ribosomal subunit. Using filter binding assays, S8 proteins from mesophilic, and (hyper)thermophilic species of the archaeal genus Methanococcus and from the bacteria Escherichia coli and Thermus thermophilus were tested for their affinity to their specific 16S rRNA target site. S8 proteins from hyperthermophiles exhibit a 100‐fold and S8 from thermophiles exhibit a 10‐fold higher affinity than their mesophilic counterparts. Thus, there is a striking correlation of affinity of S8 proteins for their specific RNA binding site and the optimal growth temperatures of the respective organisms. The stability of individual rRNA‐protein complexes might modulate the stability of the ribosome, providing a maximum of thermostability and flexibility at the growth temperature of the organism.