Biosynthesis of Phage-specific Initiation Dipeptides

The tRNA-Dependent Biosynthesis of Modified Cyclic Dipeptides

In recent years it has become apparent that aminoacyl-tRNAs are not only crucial components involved in protein biosynthesis, but are also used as substrates and amino acid donors in a variety of other important cellular processes, ranging from bacterial cell wall biosynthesis and lipid modification to protein turnover and secondary metabolite assembly. In this review, we focus on tRNA-dependen...

Initiation characteristics for the synthesis of five T4 phage-specific messenger RNAs in vitro.

The involvement of the nucleoside triphosphates in the initiation of the synthesis of the messenger ribonucleic acid of five T4 specific enzymes has been studied. Only one of these, the messenger RNA for deoxynucleosidemonophosphate kinase, can be initiated in the presence of one nucleoside triphosphate, namely ATP. All of the remaining four require the presence of at least two nucleoside triph...

Identification of a Specific Pseudo attP Site for Phage PhiC31 Integrase in Bovine Genome

Background: PhiC31 integrase system provides a new platform in various felid of research, mainly in gene therapy and creation of transgenic animals. This system enables integration of exogenous DNA into preferred locations in mammalian genomes, which results in robust, long-term expression of the integrated transgene. Objectives: Identification of a novel pseudo attP site. Materials and Methods...

Initiation of Methylglucose Lipopolysaccharide Biosynthesis in Mycobacteria

BACKGROUND Mycobacteria produce two unique families of cytoplasmic polymethylated polysaccharides -- the methylglucose lipopolysaccharides (MGLPs) and the methylmannose polysaccharides (MMPs) -- the physiological functions of which are still poorly defined. Towards defining the roles of these polysaccharides in mycobacterial physiology, we generated knock-out mutations of genes in their putativ...

Phage activation by prolyl isomerization Initiation of phage infection by partial unfolding and prolyl isomerization*