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Endoreduplication (also referred to as endoreplication or endocycling) is replication of the nuclear genome in the absence of mitosis, which leads to elevated nuclear gene content and polyploidy.
Chemical structure of an LNA monomer an additional bridge bonds the 2' oxygen and the 4' carbon of the pentose. A locked nucleic acid (LNA), also known as bridged nucleic acid (BNA), [1] and often referred to as inaccessible RNA, is a modified RNA nucleotide in which the ribose moiety is modified with an extra bridge connecting the 2' oxygen and 4' carbon.
In one study, the characteristic C3'-endo pucker is found on the first three sugars of the DNA strand, while the last three sugars have a C2'-endo pucker, like B-DNA. [2] These intermediates can form in aqueous solutions when the cytosine bases are methylated or brominated, altering the conformation.
H/ACA snoRNAs also contain conserved sequence motifs known as H box (consensus ANANNA) and the ACA box (ACA). Both motifs are usually located in the single-stranded regions of the secondary structure. The H motif is located in the hinge and the ACA motif is located in the tail region; 3 nucleotides from the 3′ end of the sequence. [11]
Double-stranded DNA phage lysins tend to lie within the 25 to 40 kDa range in terms of size. A notable exception is the streptococcal PlyC endolysin, which is 114 kDa. PlyC is not only the biggest and most potent lysin, but also structurally unique since it is composed of two different gene products, PlyCA and PlyCB, with a ratio of eight PlyCB subunits for each PlyCA in its active conformation.
Those that reach the inside of the endoplasmic reticulum are folded into the correct three-dimensional conformation. Chemicals, such as carbohydrates or sugars, are added, then the endoplasmic reticulum either transports the completed proteins, called secretory proteins, to areas of the cell where they are needed, or they are sent to the Golgi ...
[1] [2] [3] The endonuclease activity of FENs was initially identified as acting on a DNA duplex which has a single-stranded 5' overhang on one of the strands [4] (termed a "5' flap", hence the name flap endonuclease [5]). FENs catalyse hydrolytic cleavage of the phosphodiester bond at the junction of single- and double-stranded DNA. [6]
Glycoside hydrolases can also be classified as exo or endo acting, dependent upon whether they act at the (usually non-reducing) end or in the middle, respectively, of an oligo/polysaccharide chain. Glycoside hydrolases may also be classified by sequence or structure-based methods. [7]