Substrate Recognition by the Leucyl/Phenylalanyl-tRNA-protein Transferase
Substrate Recognition by the Leucyl/Phenylalanyl-tRNA-protein Transferase
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亮氨酰/苯丙氨酰-tRNA-蛋白转移酶的底物识别
DOI：
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发表时间：
1997
影响因子：
4.8
通讯作者：
T. E. Shrader
中科院分区：
文献类型：
--
作者：
I. Ichetovkin;G. Abramochkin;T. E. Shrader
来自大肠杆菌的亮氨酰/苯丙氨酰-tRNA-蛋白转移酶（L/F-转移酶）催化肽基转移酶反应，该反应导致受体蛋白的N-末端氨酰化，使用Leu-、Phe-和Met-tRNA作为氨基酸供体。我们证明，L/F-转移酶同系物广泛分布在整个真细菌，支持我们的建议，酶家族是古老的，催化早期的肽键合成。然而，在这里，我们提出的数据表明，L/F-转移酶是不是在革兰氏阳性菌，如金黄色葡萄球菌的细胞壁肽聚糖生物合成中涉及的肽基转移酶的同系物。已知的L/F-转移酶同源物的序列比较开始鉴定催化肽基转移酶反应所需的必需残基，并揭示<20%的残基在L/F-转移酶家族内是不变的。尽管有这种序列变异，底物特异性是广泛保守的，来自斯氏普罗威登斯菌、霍乱弧菌、淋病奈瑟菌和蓝细菌集胞藻的L/F-转移酶同系物都与大肠杆菌互补。coli aat突变体（缺乏L/F-转移酶活性）用于降解N-末端规则底物。在体外比较了弗罗姆.大肠杆菌和蓝细菌集胞藻属，揭示了底物特异性和二级结构的几乎完全保守。最后，我们证明了E.大肠杆菌L/F-转移酶，缺乏33或78个N-末端残基，保留可测量的肽基转移酶活性和野生型底物特异性。总的来说，我们的研究结果确定了一个L/F-转移酶的基本核心，并揭示了肽基转移酶催化剂可以从120个氨基酸构建。
The leucyl/phenylalanyl-tRNA-protein transferase (L/F-transferase) from Escherichia coli catalyzes a peptidyltransferase reaction that results in the N-terminal aminoacylation of acceptor proteins using Leu-, Phe-, and Met-tRNAs as amino acid donors. We demonstrated that L/F-transferase homologs are widely distributed throughout the eubacteria, supporting our proposal that the enzyme family is ancient and catalyzes early peptide bond synthesis. However, here we present data suggesting that the L/F-transferase is not a homolog of the peptidyltransferase enzymes involved in cell wall peptidoglycan biosynthesis in Gram-positive species, such as Staphylococcus aureus. A sequence comparison of the known L/F-transferase homologs began to identify the essential residues required to catalyze a peptidyltransferase reaction and revealed that <20% of the residues were invariant within the L/F-transferase family. Despite this sequence variation, substrate specificity was broadly conserved, and L/F-transferase homologs from Providencia stuartii,Vibrio cholerae, Neisseria gonorrhoeae, and the cyanobacterium Synechocystis sp. all complemented an E. coli aat mutant (lacking L/F-transferase activity) for the degradation of N-end rule substrates. In vitrocomparison of the most divergent L/F-transferase homologs, fromE. coli and the cyanobacterium Synechocystissp., revealed near-complete conservation of both substrate specificity and secondary structure. Finally, we demonstrated that variants of theE. coli L/F-transferase, lacking either 33 or 78 N-terminal residues, retained measurable peptidyltransferase activity and wild type substrate specificity. Overall, our results identified an essential core of an L/F-transferase and revealed that a peptidyltransferase catalyst may be constructed from ∼120 amino acids.
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影响因子：
10.5
作者：
Siegele,DA;Kolter,R
通讯作者：
Kolter,R
影响因子：
56.9
作者：
TOBIAS, JW;SHRADER, TE;VARSHAVSKY, A
通讯作者：
VARSHAVSKY, A
DOI：
10.1073/pnas.85.4.1033
发表时间：
1988-02-01
影响因子：
11.1
作者：
SAMPSON, JR;UHLENBECK, OC
通讯作者：
UHLENBECK, OC
DOI：
10.1016/s0021-9258(19)39136-7
发表时间：
1990-05
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
E. Balzi;M. Choder;Wei Ning Chen;Alexander Varshavsky;André Goffeau
通讯作者：
E. Balzi;M. Choder;Wei Ning Chen;Alexander Varshavsky;André Goffeau
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DOI：
--
发表时间：
1994
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Gordon,CL;Sather,SK;Casjens,S;King,J
通讯作者：
King,J