[vc_empty_space][vc_empty_space]
Mutant of Y410A on AMRLY motif of yeast eRF1 enhance suppression of nonsense codons in Saccharomyces cerevisiae
Susilowati P.E.a, Aditiawati P.b, Madayanti F.b, Akhmalokab
a Department of Chemistry, University of Halouleo, Kendari, Indonesia
b School of Life Science and Technology, Institut Teknologi Bandung, Indonesia
[vc_row][vc_column][vc_row_inner][vc_column_inner][vc_separator css=”.vc_custom_1624529070653{padding-top: 30px !important;padding-bottom: 30px !important;}”][/vc_column_inner][/vc_row_inner][vc_row_inner layout=”boxed”][vc_column_inner width=”3/4″ css=”.vc_custom_1624695412187{border-right-width: 1px !important;border-right-color: #dddddd !important;border-right-style: solid !important;border-radius: 1px !important;}”][vc_empty_space][megatron_heading title=”Abstract” size=”size-sm” text_align=”text-left”][vc_column_text]© IJIB, All rights reserved.The termination of translation in Saccharomyces cerevisiae is controlled by two interacting polypeptide chain release factors, eRF1 and eRF3. Two regions in eRF1, at position 281-305 and at position 411-415, were proposed to be involved on the interaction to eRF3. In this study we have constructed and characterized eRF1 mutant at position 410 from tyrosine to alanine residue, namely eRF1(Y410A) respectively. The mutation did not affect the viability or temperature sensitivity of the cell. The stop codons readthrough of the mutant was analyzed in vivo using PGK-stop codon-LACZ gene fusion and the results showed that the suppression of the mutant was increased in all of the codon terminations. The suppression of the UAG codon was the highest increased among the stop codons by comparing to the suppression of the wild type respectively. Computer modeling analysis using Swiss-Prot and Amber version 9.0 programs revealed that the overall structure of eRF1 mutant has no significant difference with the wild type. Detail analysis of the third domain of eRF1 (Y410A) was also confirmed that there was no structural alteration on the region. This suggests that defecting of the eRF1(Y410A) to terminate the protein biosynthesis was not due to the structural change of eRF1 but rather than the substitution of tyrosine to alanine.[/vc_column_text][vc_empty_space][vc_separator css=”.vc_custom_1624528584150{padding-top: 25px !important;padding-bottom: 25px !important;}”][vc_empty_space][megatron_heading title=”Author keywords” size=”size-sm” text_align=”text-left”][vc_column_text][/vc_column_text][vc_empty_space][vc_separator css=”.vc_custom_1624528584150{padding-top: 25px !important;padding-bottom: 25px !important;}”][vc_empty_space][megatron_heading title=”Indexed keywords” size=”size-sm” text_align=”text-left”][vc_column_text]eRF1,GIRLY motif,Mutation,Nonsense codon suppression,Saccharomyces cerevisiae[/vc_column_text][vc_empty_space][vc_separator css=”.vc_custom_1624528584150{padding-top: 25px !important;padding-bottom: 25px !important;}”][vc_empty_space][megatron_heading title=”Funding details” size=”size-sm” text_align=”text-left”][vc_column_text][/vc_column_text][vc_empty_space][vc_separator css=”.vc_custom_1624528584150{padding-top: 25px !important;padding-bottom: 25px !important;}”][vc_empty_space][megatron_heading title=”DOI” size=”size-sm” text_align=”text-left”][vc_column_text][/vc_column_text][/vc_column_inner][vc_column_inner width=”1/4″][vc_column_text]Widget Plumx[/vc_column_text][/vc_column_inner][/vc_row_inner][/vc_column][/vc_row][vc_row][vc_column][vc_separator css=”.vc_custom_1624528584150{padding-top: 25px !important;padding-bottom: 25px !important;}”][/vc_column][/vc_row]