ABC50 mutants modify translation start codon selection.

ABC50 mutants modify translation start codon selection.
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ABC50 突变体修改翻译起始密码子选择。

DOI:
10.1042/bj20141453
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发表时间:
2015
期刊:
The Biochemical journal
影响因子:
--
通讯作者:
Stewart JD
Stewart JD
中科院分区:
--
文献类型:
--
作者:
Stewart JD

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atp结合盒50 (ABC50,也称为ABCF1)与真核起始因子2 (eIF2)结合,是高效翻译起始所必需的。起始密码子的准确识别和选择是这一过程的关键。人们普遍认为,eIF1、eIF1A和eIF5的存在和运动是调节起始位点选择的严格性的关键因素,而起始位点选择通常需要一个AUG密码子在合适的序列环境中。在本研究中,我们发现不能水解ATP的ABC50突变体的表达减少了一般翻译,并放松了对在翻译起始位点使用非aug密码子的歧视。这些突变体似乎不会改变关键起始因子与40S亚基的关联。通过过表达eIF1可以恢复起始位点选择的严格性,这与该因子增强严格性的作用是一致的。本研究表明,干扰ABC50的功能会影响起始密码子选择的准确性。
ATP-binding cassette 50 (ABC50; also known as ABCF1) binds to eukaryotic initiation factor 2 (eIF2) and is required for efficient translation initiation. An essential step of this process is accurate recognition and selection of the initiation codon. It is widely accepted that the presence and movement of eIF1, eIF1A and eIF5 are key factors in modulating the stringency of startsite selection, which normally requires an AUG codon in an appropriate sequence context. In the present study, we show that expression of ABC50 mutants, which cannot hydrolyse ATP, decreases general translation and relaxes the discrimination against the use of non-AUG codons at translation start sites. These mutants do not appear to alter the association of key initiation factors to 40S subunits. The stringency of start-site selection can be restored through overexpression of eIF1, consistent with the role of that factor in enhancing stringency. The present study indicates that interfering with the function of ABC50 influences the accuracy of initiation codon selection.
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