| Yazarlar (4) |
Dr. Öğr. Üyesi Fatemeh MOLLAAMIN
|
M. Noei
|
|
M. Monajjemi
|
|
R. Rasoolzadeh
|
| Özet |
| It is generally accepted that initiation of protein synthesis in Escherichia coli starts with formyl-methionine, directed by the codons AUG or GUG. Protein synthesis proceeds by transfer of the growing polypeptide chain from the tRNA bound to the ribosomal P site to the incoming aminoacyl-tRNA in the adjacent A site. After translocation of the ribosome in the 30 direction of the mRNA, by the action of elongation factor G, the A site again becomes empty and the next codon exposed so that a new aminoacyl-tRNA ternary complex can be selected (Ogle and Ramakrishnan, 2005).Synthetic polynucleotide containing AUG and/or GUG codons as well as natural mRNA have been used extensively in order to elucidate the mechanism of initiation of protein synthesis (Grunberg-Manago, 1977). In all these studies it has been assumed that binding of fMet-tRNA to ribosome’s is the polynucleotide in bacteria the start codon AUG is recognized by fMet-tRNA. This tRNA does not recognize internal AUG codons. Initiation of protein biosynthesis requires the correct positioning of charged initiator tRNA, fMet-tRNA in the ribosomal P-site of the mRNA-programmed 70S ribosome’s (Gualerzi and Pon, 1990; La Teana et al., 1996; Monajjemi et al., 2008; Spurio et al., 1993; Forster et al., 1999). The rapid development of molecular biology in recent years has been mirrored by the rapid development of |
| Anahtar Kelimeler |
| Natural bond orbital (NBO) | fMet-tRNA | NMR | Opt | SCRF | fAla-tRNA |
| Makale Türü | Özgün Makale |
| Makale Alt Türü | ESCI dergilerinde yayınlanan tam makale |
| Dergi Adı | AFRICAN JOURNAL OF MICROBIOLOGY RESEARCH |
| Dergi ISSN | 1996-0808 |
| Dergi Tarandığı Indeksler | |
| Makale Dili | İngilizce |
| Basım Tarihi | 09-2011 |
| Cilt No | 5 |
| Sayı | 18 |
| Sayfalar | 2667 / 2674 |
