mRNA secondary structure in an open reading frame reduces translation efficiency in Bacillus subtilis.
AUTOR(ES)
Kubo, M
RESUMO
The structural gene for thermostable neutral protease, nprM, has only one stacking region, whose energy is -16.3 kcal/mol (-68.2 kJ/mol). Mutations for increasing (-30.8 kcal/mol [128.9 kJ/mol] and decreasing (-5.0 kcal/mol [-20.9 kJ/mol]) the energy of the stacking region were introduced in nprM on the recombinant plasmid pMK1 by using site-directed mutagenesis without any amino acid substitutions. The resultant plasmids were designated pMK2 and pMK3, respectively. The enzyme productivity of the pMK2 carrier was about 40% lower than that of pMK1, whereas the productivity of the pMK3 carrier was about 5% higher. The higher the stability of the stacking regions, the lower the enzyme productivity that was observed. mRNA concentrations were almost the same in the cells harboring these three plasmids. These results indicate that the secondary structure of mRNA reduces the translation efficiency.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=210167Documentos Relacionados
- Translation of the mRNA for the sporulation gene spoIIID of Bacillus subtilis is dependent upon translation of a small upstream open reading frame.
- Induced mRNA stability in Bacillus subtilis.
- Light modulation of ferredoxin mRNA abundance requires an open reading frame.
- Chloramphenicol induces translation of the mRNA for a chloramphenicol-resistance gene in Bacillus subtilis.
- Upstream Open Reading Frames as Regulators of mRNA Translation