从大肠杆菌中分离出F1 ATP酶α亚基的第四个含半胱氨酸肽需要对DNA序列进行修正。
Isolation of a fourth cysteinyl-containing peptide of the alpha-subunit of the F1 ATPase from Escherichia coli necessitates revision of the DNA sequence.
作者信息
Stan-Lotter H, Clarke D M, Bragg P D
出版信息
FEBS Lett. 1986 Mar 3;197(1-2):121-4. doi: 10.1016/0014-5793(86)80310-6.
The rapid determination of cysteinyl residues by Creighton's method [(1980) Nature 284, 487-489] led to the discovery of a discrepancy between protein and DNA sequence data in the alpha-subunit of the F1 ATPase from Escherichia coli [(1984) Arch. Biochem. Biophys. 229, 320-328]. We have isolated a cysteinyl-containing decapeptide from the alpha-subunit with a protein sequence (AGCAMGEYFR) which is only partially recognizable from DNA data. Re-sequencing of DNA in the region coding for the peptide has resulted in two corrections: insertion of a cytosine before position 715 and deletion of a thymine at position 731 of the uncA gene.
采用克赖顿方法[（1980年）《自然》284卷，487 - 489页]对半胱氨酰残基进行快速测定，结果发现在来自大肠杆菌的F1 ATP酶α亚基的蛋白质和DNA序列数据之间存在差异[（1984年）《生物化学与生物物理学报》229卷，320 - 328页]。我们已从α亚基中分离出一种含半胱氨酰的十肽，其蛋白质序列为（AGCAMGEYFR），而该序列仅能从DNA数据中部分识别。对编码该肽段区域的DNA重新测序带来了两处校正：在uncA基因的715位之前插入一个胞嘧啶，并在731位缺失一个胸腺嘧啶。
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