In contrast, only 3.4% of the reads were assigned to eukaryotes and almost no viral sequence was detectable in BE-1, but eukaryotic and viral detections were significantly increased to 20.5% and 9.3% in BEY, respectively.
N-terminal N-myristoylation is a lipid anchor modification of eukaryotic and viral proteins targeting them to membrane locations, thus changing the cellular function of modified proteins.
Studies with model gene systems, and a variety of eukaryotic and viral transcription factors, have shown that these molecules are potent inhibitors of protein DNA interactions.
It consists in the high-throughput sequencing of a pool of DNA fragments that may encompass various genomic loci from all taxa represented in the sample (prokaryotic, eukaryotic, and viral genomes).
Myristoyl-CoA protein N-Myristoyl-CoA protein(Nmt) is a monomeric enzyme that catalyzes the transfer of the fatty acid myristate from myristoyl-CoA to the Nmtermisal glycine residue of a variety of eukaryotic and viral proteins.
N-myristoylation is a crucial covalent modification of numerous eukaryotic and viral proteins that is catalyzed by N-myristoyltransferase (NMT).
Actually, among these 83 proteins, we found that 16, 1, 33, and 12 CroV proteins showed bacterial, archaeal, eukaryotic, and viral homologs, respectively (Figure S1).
Following the discovery of N-myristoylation by Carr et al. [3] numerous N-myristoylated eukaryotic and viral proteins have been identified (reviewed in [1], [4]).
The three isoforms of polypyrimidine tract binding protein (PTB1, 2 and 4) [6] [7], La protein[8], and upstream of n-ras protein (unr) [9] are examples of ITAFs required for efficient translation from eukaryotic and viral IRESes.
This, in principle, enables the measurement of the proportions of bacterial, archaeal, eukaryotic and viral sequences.
