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Characterization of a Functionally Unknown Arginine-Aspartate-Aspartate Family Protein From Halobacillus andaensis and Functional Analysis of Its Conserved Arginine/Aspartate Residues.


ABSTRACT: Arginine-aspartate-aspartate (RDD) family, representing a category of transmembrane proteins containing one highly conserved arginine and two highly conserved aspartates, has been functionally uncharacterized as yet. Here we present the characterization of a member of this family designated RDD from the moderate halophile Halobacillus andaensis NEAU-ST10-40T and report for the first time that RDD should function as a novel Na+(Li+, K+)/H+ antiporter. It's more interesting whether the highly conserved arginine/aspartate residues among the whole family or between RDD and its selected homologs are related to the protein function. Therefore, we analyzed their roles in the cation-transporting activity through site-directed mutagenesis and found that D154, R124, R129, and D158 are indispensable for Na+(Li+, K+)/H+ antiport activity whereas neither R35 nor D42 is involved in Na+(Li+, K+)/H+ antiport activity. As a dual representative of Na+(Li+, K+)/H+ antiporters and RDD family proteins, the characterization of RDD and the analysis of its important residues will positively contribute to the knowledge of the cation-transporting mechanisms of this novel antiporter and the roles of highly conserved arginine/aspartate residues in the functions of RDD family proteins.

SUBMITTER: Shao L 

PROVIDER: S-EPMC5996927 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature

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Characterization of a Functionally Unknown Arginine-Aspartate-Aspartate Family Protein From <i>Halobacillus andaensis</i> and Functional Analysis of Its Conserved Arginine/Aspartate Residues.

Shao Li L   Abdel-Motaal Heba H   Chen Jin J   Chen Huiwen H   Xu Tong T   Meng Lin L   Zhang Zhenglai Z   Meng Fankui F   Jiang Juquan J  

Frontiers in microbiology 20180425


Arginine-aspartate-aspartate (RDD) family, representing a category of transmembrane proteins containing one highly conserved arginine and two highly conserved aspartates, has been functionally uncharacterized as yet. Here we present the characterization of a member of this family designated RDD from the moderate halophile <i>Halobacillus andaensis</i> NEAU-ST10-40<sup>T</sup> and report for the first time that RDD should function as a novel Na<sup>+</sup>(Li<sup>+</sup>, K<sup>+</sup>)/H<sup>+</  ...[more]

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