大肠杆菌YegI是一种新的丝氨酸/苏氨酸激酶,缺乏保守的基元,定位于内膜。

IF 3 4区 生物学 Q3 BIOCHEMISTRY & MOLECULAR BIOLOGY FEBS Letters Pub Date : 2020-11-01 Epub Date: 2020-09-13 DOI:10.1002/1873-3468.13920
Krithika Rajagopalan, Jonathan Dworkin
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引用次数: 5

摘要

在细菌中,信号磷酸化被认为主要发生在His和Asp残基上。然而,在过去的十年中,对系统发育多样的细菌的磷酸化蛋白质组学调查已经发现了许多在丝氨酸和/或苏氨酸残基上磷酸化的蛋白质。一致地,编码丝氨酸/苏氨酸激酶的基因存在于许多细菌基因组中,如大肠杆菌基因组,它编码至少三种丝氨酸/苏氨酸激酶。在这里,我们鉴定了一个以前未被表征的ORF, yegI,并证明它编码一种新的丝氨酸/苏氨酸激酶。YegI缺乏几个保守的基序,包括在其他细菌丝氨酸/苏氨酸激酶中看到的对Mg2+结合重要的残基,这表明共识可能过于严格。我们进一步发现YegI是一种双通道膜蛋白,其N端和C端都位于细胞内。
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Escherichia coli YegI is a novel Ser/Thr kinase lacking conserved motifs that localizes to the inner membrane.

In bacteria, signaling phosphorylation is thought to occur primarily on His and Asp residues. However, phosphoproteomic surveys in phylogenetically diverse bacteria over the past decade have identified numerous proteins that are phosphorylated on Ser and/or Thr residues. Consistently, genes encoding Ser/Thr kinases are present in many bacterial genomes such as in the Escherichia coli genome, which encodes at least three Ser/Thr kinases. Here, we identify a previously uncharacterized ORF, yegI, and demonstrate that it encodes a novel Ser/Thr kinase. YegI lacks several conserved motifs including residues important for Mg2+ binding seen in other bacterial Ser/Thr kinases, suggesting that the consensus may be too stringent. We further find that YegI is a two-pass membrane protein with both N- and C termini located intracellularly.

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来源期刊
FEBS Letters
FEBS Letters 生物-生化与分子生物学
CiteScore
6.60
自引率
2.90%
发文量
303
审稿时长
1 months
期刊介绍: FEBS Letters is one of the world''s leading journals in molecular biology and is renowned both for its quality of content and speed of production. Bringing together the most important developments in the molecular biosciences, FEBS Letters provides an international forum for Minireviews, Research Letters and Hypotheses that merit urgent publication.
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