Aminoacylation of an Unusual TRNA(Cys) from an Extreme Halophile

Overview

Journal RNA

Specialty Molecular Biology

Date 2003 Jun 18

PMID 12810913

Citations 5

Authors

Caryn Evilia

Xiaotian Ming

Shiladitya DasSarma

Ya-Ming Hou

Affiliations

Soon will be listed here.

Abstract

The extreme halophile Halobacterium species NRC-1 overcomes external near-saturating salt concentrations by accumulating intracellular salts comparable to those of the medium. This raises the fundamental question of how halophiles can maintain the specificity of protein-nucleic acid interactions that are particularly sensitive to high salts in mesophiles. Here we address the specificity of the essential aminoacylation reaction of the halophile, by focusing on molecular recognition of tRNA(Cys) by the cognate cysteinyl-tRNA synthetase. Despite the high salt environments of the aminoacylation reaction, and despite an unusual structure of the tRNA with an exceptionally large dihydrouridine loop, we show that aminoacylation of the tRNA proceeds with a catalytic efficiency similar to that of its mesophilic counterparts. This is manifested by an essentially identical K(m) for tRNA to those of the mesophiles, and by recognition of the same nucleotide determinants that are conserved in evolution. Interestingly, aminoacylation of the halophile tRNA(Cys) is more closely related to that of bacteria than eukarya by placing a strong emphasis on features of the tRNA tertiary core. This suggests an adaptation to the highly negatively charged tRNA sugar-phosphate backbone groups that are the key elements of the tertiary core.

Citing Articles

Dynamic structure mediates halophilic adaptation of a DNA polymerase from the deep-sea brines of the Red Sea.

Takahashi M, Takahashi E, Joudeh L, Marini M, Das G, Elshenawy M FASEB J. 2018; 32(6):3346-3360.

PMID: 29401622 PMC: 6051491. DOI: 10.1096/fj.201700862RR.

Circular dichroism and fluorescence spectroscopy of cysteinyl-tRNA synthetase from Halobacterium salinarum ssp. NRC-1 demonstrates that group I cations are particularly effective in providing structure and stability to this halophilic protein.

Reed C, Bushnell S, Evilia C PLoS One. 2014; 9(3):e89452.

PMID: 24594651 PMC: 3940603. DOI: 10.1371/journal.pone.0089452.

Protein adaptations in archaeal extremophiles.

Reed C, Lewis H, Trejo E, Winston V, Evilia C Archaea. 2013; 2013:373275.

PMID: 24151449 PMC: 3787623. DOI: 10.1155/2013/373275.

Function and biotechnology of extremophilic enzymes in low water activity.

Karan R, Capes M, DasSarma S Aquat Biosyst. 2012; 8(1):4.

PMID: 22480329 PMC: 3310334. DOI: 10.1186/2046-9063-8-4.

Post-genomics of the model haloarchaeon Halobacterium sp. NRC-1.

DasSarma S, Berquist B, Coker J, DasSarma P, Muller J Saline Syst. 2006; 2:3.

PMID: 16542428 PMC: 1447603. DOI: 10.1186/1746-1448-2-3.

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