Abstract
Protein has been known as an important macromolecule which has a vital role among the living organism. One of the most interesting protein is Arc1p, which is a yeast-specific tRNA-binding protein. Arc1p is a unique protein that has the ability to form a ternary complex with glutamyl-tRNA synthetase (GluRS c ) and methionyl-tRNA synthetase (MetRS) in the cytoplasm. This complex can significantly enhance the aminoacylation efficiency of these two aaRSs to their respective cognate tRNAs. Recently, it was found that Arc1p can be biotinylated via post-translational modification at Lys86 (K86) in the N-domain. Here, we try to figure it out what kind of method that will help to create some clear information both in structure and function of this protein, when mutations occur inside of the K86 site within SSKD motifs of Arc1p. Several methods to better understanding obviously about protein characteristics comprises protein structural analysis; such as gel mobility shift assay, CD Spectroscopy, and limited proteolysis; protein functional analysis, and in silico modeling . Keywords : Arc1p, biotinylation, function, in silico , structure.
Highlights
Protein is an important macromolecule which has an indispensable role in the widely living organism
Cofactor 1) is a yeast-specific tRNA-binding protein that has the ability to make a ternary complex with glutamyl-tRNA synthetase (GluRSc) and methionyl-tRNA synthetase (MetRS) in the cytoplasm
Arc1p defined as yeast-specific tRNA-binding protein and has the primary ability to make a ternary complex with glutamyl-tRNA synthetase (GluRSc) and methionyl-tRNA synthetase (MetRS) in the cytoplasm [3]
Summary
Protein is an important macromolecule which has an indispensable role in the widely living organism. In order to measure the relative biotinylation levels of Arc1p variants from WT and yeast mutants, a streptavidin-based gel mobility shift assay was determined [4] This phenomenon was based on due to the almost irreversible binding of biotin with streptavidin (Kd = 10-14 M) [5]. Reported that avidin has a tighter binding of biotin than streptavidin (Kd =6 x 10-16 and 4 x 10-14 M, respectively) [8] In this case, CD Spectroscopy was used in order to investigate whether biotinylation affects the secondary structure of Arc1p variants. Most widely applied of circular dichroism are for study the secondary structure of proteins, such as the α‐helix and the β sheet (Fig. 3) This method allows us to explore deeper the higher order structures of chiral macromolecules including proteins and DNA. After the treatment of trypsin, the result will be obtained which Arc1p is more flexible in term of structure than the others
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