Single Mutation in Shine-Dalgarno-Like Sequence Present in the Amino Terminal of Lactate Dehydrogenase of Plasmodium Effects the Production of an Eukaryotic Protein Expressed in a Prokaryotic System

  title={Single Mutation in Shine-Dalgarno-Like Sequence Present in the Amino Terminal of Lactate Dehydrogenase of Plasmodium Effects the Production of an Eukaryotic Protein Expressed in a Prokaryotic System},
  author={Mustafa Çiçek and Ozal Mutlu and Aysegul Demirhan Erdemir and Ebru Ozkan and Yunus Sariçay and Dilek Turgut-Balik},
  journal={Molecular Biotechnology},
One of the most important step in structure-based drug design studies is obtaining the protein in active form after cloning the target gene. In one of our previous study, it was determined that an internal Shine-Dalgarno-like sequence present just before the third methionine at N-terminus of wild type lactate dehydrogenase enzyme of Plasmodium falciparum prevent the translation of full length protein. Inspection of the same region in P. vivax LDH, which was overproduced as an active enzyme… 
Characterization of the internal translation initiation region in monoclonal antibodies expressed in Escherichia coli
Using computational and biochemical approaches, it is demonstrated that an internal translation initiation from a GTG codon within eNISTmAb results from a weak Shine–Dalgarno sequence and is facilitated by a putative ribosomal protein S1-binding site.


Determination of the DNA and Amino Acid Sequences of the Lactate Dehydrogenase Gene from Plasmodium falciparum Strains K1 and PF FCBR: A Route to the Design of New Antimalarials
Cl cloning of the gene coding for the lactate dehydrogenase (LDH) gene from the two different strains of Plasmodium falciparum, K1 and PF FCBR shows that PfLDH has a five residue insertion in the catalytic loop compared to other LDH sequences, which could be exploited in drug design.
Over-production of lactate dehydrogenase from Plasmodium falciparum opens a route to new antimalarials
The high-resolution X-ray structure obtained from the recombinant enzyme has provided the opportunity for the development of inhibitors specific to PfLDH.
Cloning, sequence and expression of the lactate dehydrogenase gene from the human malaria parasite, Plasmodium vivax
Structural differences between human LDHs and PfLDH make the latter an attractive target for inhibitors leading to novel anti-malarial drugs, and sequence similarity between PvLDH and Pf LDH indicate that the same approach could be applied to Plasmodium vivax, the most common human malaria parasite in the world.
Heterologous expression of proteins from Plasmodium falciparum: results from 1000 genes.
A Plausible Role for the Presence of Internal Shine-Dalgarno Sites
  • L. Ponnala
  • Biology, Computer Science
    Bioinformatics and biology insights
  • 2010
This paper detects the presence of nucleotide hybridization sites inside the coding regions of E. coli genes, and analyzes their proximity to clusters of slow-translating codons to propose an explanation for the existence of RNA hybridization within the translated regions of bacterial genes.
Expression of Plasmodium falciparum lactate dehydrogenase in Escherichia coli.
Correlations between Shine-Dalgarno Sequences and Gene Features Such as Predicted Expression Levels and Operon Structures
A significant positive correlation of the presence of an SD sequence and the predicted expression level of a gene based on codon usage biases was ascertained, such that predicted highly expressed genes are more likely to possess a strong SD sequence than average genes.
The effect of ribosomal protein S1 from Escherichia coli and Micrococcus luteus on protein synthesis in vitro by E. coli and Bacillus subtilis
The presence of a strong SD sequence alone is able to substitute for at least part of the activities of ribosomal protein S1, and that ribosomes that exhibit S1 ‐independent translation on such messages also show less reliance on AUG as an initiation codon.
The Genome of the Kinetoplastid Parasite, Leishmania major
The organization of protein-coding genes into long, strand-specific, polycistronic clusters and lack of general transcription factors in the L. major, Trypanosoma brucei, and Tritryp genomes suggest that the mechanisms regulating RNA polymerase II–directed transcription are distinct from those operating in other eukaryotes, although the trypanosomatids appear capable of chromatin remodeling.