A Single Glutamate Residue Controls the Oligomerization, Function, and Stability of the Aquaglyceroporin GlpF

Florian Cymer and Dirk Schneider

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A Single Glutamate Residue Controls the Oligomerization, Function, and Stability of the Aquaglyceroporin GlpF

机译：一个单一的谷氨酸残基控制水甘油糖蛋白GlpF的齐聚，功能和稳定性。

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Like many other R-helical membrane proteins, the monomeric Escherichia coli aquaglyceroporinnGlpF associates within cellular membranes and forms higher-order oligomeric structures. A potential impactnof the oligomeric state on the protein function remains enigmatic.We have analyzed the role of residuesW42nand E43 in the oligomerization of the E. coli GlpF protein in vitro and in vivo. In contrast toW42, the polarnglutamate residue at position 43 appears to be critical for oligomerization. While other polar residues cannsubstitute for the function of E43, replacement of E43 with alanine results in a greatly reduced GlpFnoligomerization propensity. The reduced interaction propensity of GlpF E43A correlates with an impaired innvivo function aswell as a decreased in vivo stability. Therefore, E43 is critical for the proper oligomerization ofnGlpF, and protein oligomerization appears to be crucial for the channel function as well as for the in vivonstability of the protein.

机译：像许多其他R螺旋膜蛋白一样，单体大肠杆菌aquaglyceroporinnGlpF在细胞膜内结合并形成更高阶的寡聚结构。寡聚状态对蛋白质功能的潜在影响仍然是未知的。我们已经分析了残基W42n和E43在体外和体内大肠杆菌GlpF蛋白寡聚中的作用。与W42相反，第43位的极化谷氨酸残基似乎对寡聚反应至关重要。虽然其他极性残基不能替代E43的功能，但用丙氨酸替代E43会导致GlpFnoligomerization倾向大大降低。 GlpF E43A的相互作用倾向降低与体内功能受损以及体内稳定性降低相关。因此，E43对于nGlpF的正确寡聚化至关重要，而蛋白质寡聚化对于通道功能以及蛋白质的体内稳定性至关重要。

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《Biochemistry》 |2010年第2期|p.279-286|共8页
作者
Florian Cymer and Dirk Schneider;
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‡Institut f€ ur Biochemie und Molekularbiologie, ZBMZ and §Fakult€ at f€ ur Biologie, Albert-Ludwigs-Universit€ at Freiburg,Stefan-Meier-Strasse 17, 79104 Freiburg, Germany;

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1. A single glutamate residue controls the oligomerization, function, and stability of the aquaglyceroporin GlpF [J] . Cymer F., Schneider D. Biochemistry . 2010,第2期

机译：单个谷氨酸残基控制着水甘油糖蛋白GlpF的低聚，功能和稳定性
2. The GlpF residue Trp219 is part of an amino-acid cluster crucial for aquaglyceroporin oligomerization and function [J] . Margareta Trefz, Rebecca Keller, Miriam Vogt, Biochimica et biophysica acta. Biomembranes . 2018,第4期

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3. CORRELATED SOLVENT-INDUCED FORCES ON A PROTEIN AT SINGLE RESIDUE RESOLUTION - RELATION TO CONFORMATION, STABILITY, DYNAMICS AND FUNCTION [J] . Martorana V., Palma MU., Corongiu G. Chemical Physics Letters . 1996,第5a6期

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机译：固相氨基酸保护，肽构建和合成肽可用于定义蛋白质的稳定性，功能以及鉴定酶促活性位点的残基。
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A Single Glutamate Residue Controls the Oligomerization, Function, and Stability of the Aquaglyceroporin GlpF

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