Abstract:
:Erythromycin-induced stabilization of ermA mRNA was studied in Staphylococcus aureus, its original host background, and in Bacillus subtilis, subcloned on plasmid vectors. By RNA blot analysis it was shown that 40 nM-erythromycin specifically increased the chemical half-life of ermA mRNA from 2.5 to 17.5 minutes whereas the half-life of cat-86 mRNA was not increased by erythromycin. While expression of ermA has been shown to be induced by erythromycin at the level of translation, our studies with three ermA constitutive mutants demonstrated that mRNA stabilization in growing cells occurred independently of induced gene expression, suggesting that the stabilized mRNA was not functional for protein synthesis. Studies of ermA/lacZ fusions demonstrated that the 5' end of the mRNA was sufficient to confer stabilization. Translation of specific amino acid codons in a leader peptide located at the extreme 5' end of the mRNA was required for the erythromycin-induced stabilization as a frameshift mutation introduced into the leader peptide determinant abolished stabilization. By S1 mapping, no differences were detected in the length of the 5' or 3' end of ermA mRNA with the addition of erythromycin, indicating that the stabilized transcript was not processed at its ends.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Sandler P,Weisblum Bdoi
10.1016/0022-2836(88)90116-7subject
Has Abstractpub_date
1988-10-20 00:00:00pages
905-15issue
4eissn
0022-2836issn
1089-8638pii
0022-2836(88)90116-7journal_volume
203pub_type
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journal_title:Journal of molecular biology
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journal_title:Journal of molecular biology
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journal_title:Journal of molecular biology
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journal_title:Journal of molecular biology
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journal_title:Journal of molecular biology
pub_type: 杂志文章
doi:10.1016/0022-2836(87)90609-7
更新日期:1987-09-05 00:00:00
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journal_title:Journal of molecular biology
pub_type: 杂志文章
doi:10.1016/S0022-2836(05)80208-6
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journal_title:Journal of molecular biology
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journal_title:Journal of molecular biology
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journal_title:Journal of molecular biology
pub_type: 杂志文章
doi:10.1006/jmbi.1994.1081
更新日期:1994-01-28 00:00:00
abstract::Nuclear transport factor 2 (NTF2) mediates nuclear import of RanGDP, a central component of many nuclear trafficking pathways. NTF2 is a homodimer and each chain has independent binding sites for RanGDP and nuclear pore proteins (nucleoporins) that contain FxFG sequence repeats. We show here that the monomer-dimer dis...
journal_title:Journal of molecular biology
pub_type: 杂志文章
doi:10.1006/jmbi.2001.5136
更新日期:2001-11-30 00:00:00