Affinity of ribosomal protein S8 from mesophilic and (hyper)thermophilic archaea and bacteria for 16S rRNA correlates with the growth temperatures of the organisms.
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.
Gruber
Thomas
T
Institute of Medical Chemistry and Biochemistry, University of Innsbruck, Fritz-Pregl-Str 3, A-6020 Innsbruck, Austria.
Köhrer
Caroline
C
Lung
Birgit
B
Shcherbakov
Dmitri
D
Piendl
Wolfgang
W
D000595:Amino Acid Sequence; D001105:Archaea / Q000737:chemistry / Q000235:genetics / Q000254:growth & development*; D001419:Bacteria / Q000737:chemistry / Q000235:genetics / Q000254:growth & development*; D004926:Escherichia coli / Q000737:chemistry / Q000235:genetics / Q000254:growth & development; D017017:Methanococcus / Q000737:chemistry / Q000235:genetics / Q000254:growth & development; D011485:Protein Binding; D020871:RNA Stability; D012336:RNA, Ribosomal, 16S / Q000737:chemistry / Q000378:metabolism*; D012269:Ribosomal Proteins / Q000378:metabolism*; D016415:Sequence Alignment; D013696:Temperature; D016963:Thermus thermophilus / Q000737:chemistry / Q000235:genetics / Q000254:growth & development
D012336:RNA, Ribosomal, 16S; D012269:Ribosomal Proteins; C030254:ribosomal protein S8