Functional expression of human methionine aminopeptidase type 1 in Saccharomyces cerevisiae

被引：9
|
作者：
Dummitt, B [1 ]
Fei, Y [1 ]
Chang, YH [1 ]
机构：
[1] St Louis Univ, Sch Med, Edward A Doisy Dept Biochem & Mol Biol, St Louis, MO 63104 USA
来源：
PROTEIN AND PEPTIDE LETTERS | 2002年 / 9卷 / 04期
关键词：
protein processing; terminal methionine; zinc finger; methionine aminopeptidase;
D O I：
10.2174/0929866023408607
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
We expressed recombinant human methionine aminopeptidase type I (MAP or MetAP) in a map1 null yeast strain to determine the extent of functional complementation between the two proteins. The human MetAP1 protein fully rescued the slow growth phenotype associated with deletion of yeast MetAP1, suggesting that the yeast and human MetAP1 proteins may have similar roles in vivo. Expression of human MetAP1 in yeast has significance in understanding the function of the human protein, studying its in vivo substrate specificity, and developing specific anti-fungal drugs to target yeast MetAP1.
引用
收藏
页码：295 / 303
页数：9
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