This DNA quality was sufficient to perform amplification of a specific gene using PCR technique. Wagner CTAB protocol is largely used to extract genomic DNA from different plants, but it is not ideal in the case of cannabis resin. In our experiments, the adapted protocol was used in routine extraction of DNA from cannabis resin. The high DNA quality obtained permit downstream DNA analysis techniques such as PCR and sequencing. These techniques will contribute to the identification of the geographic AbMole Amikacin hydrate origin of seized cannabis resin conducted by the police or by Customs in checkpoints and therefore establish the connection traffic pathways. Almost all proteins in AbMole Ellipticine living cells are synthesized by the ribosome. The first amino acid during this synthesis is a formyl methionine in eubacteria and methionine in eukaryotes. In about 60-70% of newly synthesized proteins, the initiator methionine is removed by a metalloenzyme called methionine aminopeptidase. In bacteria, excision of methionine is preceded by the removal of formyl group by a deformylase. Disruption of the MetAP function is detrimental. Except for actinobacteria, all other bacterial species encode for a single map gene classified as MetAP1a. Actinomyces carry additional gene for MetAP classified as MetAP1c. The difference between MetAP1a and MetAP1c is the presence of an additional 40 residue aminoterminal extension that carries consensus SH3 binding P-X-X-P motif suggesting its capability to interact with other proteins. Except for these polyproline regions no other structural motifs have been identified in bacterial MetAPs that may participate in protein-protein or protein-nucleotide interactions. All eukaryotic proteins have been demonstrated to carry additional protein sequences apart from the catalytic region that enables them to bind to the ribosome and co-translationally remove the initiator methionine. There has been a great interest in understanding the protein synthesis and co-translational peptide modification at the ribosome exit-tunnel. Recent structure of ribosome in complex with the deformylase provided the glimpse of Nterminus of the peptide modification at the ribosome exit tunnel in bacteria. Recently, it was shown through structure and biochemistry, that bacterial MetAP associate with ribosome for co-translational removal of the initiator methionine in the same place where the deformylase would associate. We have long-term interest in understanding different genetic variants with new functional motifs in MetAPs that can link their ability to interact with other macromolecules, specifically to the ribosome. Here, we report the discovery of a novel MetAP1a found predominantly in the streptococci bacteria with two new structural motifs one of which may undergo posttranslational modification of glycosylation and phosphorylation.