Each amino acid is specified by three bases (a codon) in the mRNA, ... Ribosomes are the sites of protein synthesis in both prokaryotic and eukaryotic cells. ...
But the mRNA is not altered during translation, it acts more like a co-factor. In my view , the correct answer is not amongst those listed: The two substrates of the elongation reactions would be the nascent peptide chain and the amino acyl tRNA, with the amino acid moiety getting transferred from the amino acyl tRNA to the nascent peptide chain by the catalytic process, yielding as products the elongated peptide chain and the free tRNA.
In addition, GTP hydrolysis by elongation factors is required to move the mRNA and tRNAs along to ready the ribosome for the next round of translation, making GTP an additional substrate required for translation, though not directly involved in the transfer of the amino acid moiety.
Because The actual substrate for the addition of amino acid to the growing polypeptide chain in each round is two charged species of t RNAs. They are an aminoacyl tRNA which is the carrier of amino acid to the ribosome-mRNA complex and the peptidyl tRNA which forms the peptide linkages between the amino acids.