The Cytoplasmic Domains of Streptococcus mutans Membrane Protein Insertases YidC1 and YidC2 Confer Unique Structural and Functional Attributes to Each Paralog.
The Cytoplasmic Domains of Streptococcus mutans Membrane Protein Insertases YidC1 and YidC2 Confer Unique Structural and Functional Attributes to Each Paralog.
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DOI：
10.3389/fmicb.2021.760873
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发表时间：
2021
影响因子：
5.2
通讯作者：
Brady LJ
中科院分区：
文献类型：
--
作者：
Mishra S;Brady LJ
整合蛋白和膜锚定蛋白是牙齿致病菌变形链球菌生存和毒力的关键。细菌伴侣/插入酶YidC有助于膜蛋白易位。与大肠杆菌不同，大多数革兰氏阳性细菌含有两个YidC旁系同源物。在此，我们评估了功能上描述S的结构特征。变异株YidC 1和YidC 2。细菌YidC含有五个跨膜结构域（TMD）、两个胞质环和一个胞质尾。因为S.由于变形杆菌YidC 1（SmYidC 1）和YidC 2（SmYidC 2）胞质结构域（CD）的保守性不如TMD，我们设计了14种可能的YidC 1-YidC 2 CD结构域交换组合的异位表达。将每种菌株的生长和胁迫耐受性与异位表达未修饰的yidC 1或yidC 2的对照菌株进行比较。酸和渗透胁迫敏感性与yidC 2缺失相关。对过量锌的敏感性被进一步鉴定为Δ yidC 1表型。总体而言，YidC 1比YidC 2更好地耐受CD置换。对特定CD组合的偏好表明潜在的分子内相互作用。计算机模拟分析分别预测了YidC 1的C1和C2环之间以及YidC 2的C1环和C末端尾部之间的盐桥。贡献残基的突变概括了Δ yidC 1和Δ yidC 2相关表型。总之，这项工作揭示了YidC 1和YidC 2的不同功能属性的胞质结构域的重要性，并确定了参与结构域间相互作用的关键残基。
Integral and membrane-anchored proteins are pivotal to survival and virulence of the dental pathogen, Streptococcus mutans. The bacterial chaperone/insertase, YidC, contributes to membrane protein translocation. Unlike Escherichia coli, most Gram-positive bacteria contain two YidC paralogs. Herein, we evaluated structural features that functionally delineate S. mutans YidC1 and YidC2. Bacterial YidCs contain five transmembrane domains (TMD), two cytoplasmic loops, and a cytoplasmic tail. Because S. mutans YidC1 (SmYidC1) and YidC2 (SmYidC2) cytoplasmic domains (CD) are less well conserved than are TMD, we engineered ectopic expression of the 14 possible YidC1-YidC2 CD domain swap combinations. Growth and stress tolerance of each was compared to control strains ectopically expressing unmodified yidC1 or yidC2. Acid and osmotic stress sensitivity are associated with yidC2 deletion. Sensitivity to excess zinc was further identified as a ΔyidC1 phenotype. Overall, YidC1 tolerated CD substitutions better than YidC2. Preferences toward particular CD combinations suggested potential intramolecular interactions. In silico analysis predicted salt-bridges between C1 and C2 loops of YidC1, and C1 loop and C-terminal tail of YidC2, respectively. Mutation of contributing residues recapitulated ΔyidC1- and ΔyidC2-associated phenotypes. Taken together, this work revealed the importance of cytoplasmic domains in distinct functional attributes of YidC1 and YidC2, and identified key residues involved in interdomain interactions.
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DOI：
10.1107/s2053230x14012540
发表时间：
2014-08
期刊：
Acta crystallographica. Section F, Structural biology communications
影响因子：
--
作者：
Kumazaki K;Tsukazaki T;Nishizawa T;Tanaka Y;Kato HE;Nakada-Nakura Y;Hirata K;Mori Y;Suga H;Dohmae N;Ishitani R;Nureki O
通讯作者：
Nureki O
影响因子：
5.8
作者：
Gouet, P;Courcelle, E;Métoz, F
通讯作者：
Métoz, F
盐桥的进化稳定性暗示其对蛋白质稳定性的贡献
DOI：
10.1016/j.csbj.2019.06.022
发表时间：
2019-01-01
影响因子：
6
作者：
Ban, Xiaofeng;Lahiri, Pratik;Kaustubh, Bhalerao
通讯作者：
Kaustubh, Bhalerao
影响因子：
3.7
作者：
Galvao, Lvia C. C.;Miller, James H.;Lemos, Jose A.
通讯作者：
Lemos, Jose A.
影响因子：
4.6
作者：
Kumazaki K;Kishimoto T;Furukawa A;Mori H;Tanaka Y;Dohmae N;Ishitani R;Tsukazaki T;Nureki O
通讯作者：
Nureki O