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Gene duplication events

Phase and antigenic variation in bacteria. These may be mediated by slipped-strand mispairing of repeat sequences that occur in these phase variable genes or by gene duplication events. [Pg.19]

The three molecules of the IL-1 family, interleukin-la (IL-la), interleukin-1 3 (IL-ip), and interleukin-1 receptor antagonist (IL-IRa) map to the long arm of chromosome two in the human genome. It appears that the family arose via a gene duplication event some 350 million years ago, and the molecules possess between 27.5 and 36% sequence identity with each other (Table 2) [1,14,15]. In addition, the genes for the two IL-1 receptors IL-1R1 and IL-1RII [16,17], and an IL-1R accessory protein (IL-lRacP), which binds to the IL-1, IL-1 receptor complex [18], have been identified. Together, these molecules via their differential activity serve primarily to modulate the host defense mechanism. [Pg.398]

Fig. 9.2. Schematic illustration of the (Pa)g-barrel structure. The highly symmetrical structure presumably arose by multiple gene duplication events from a Pa-fragment. This hypothesis was tested using reverse engineering. Bisection of the barrel into two halves yielded correctly folded fragments which, upon heterodimerization, regained parental function. However, further fragmentation awaits experimental exploration. Fig. 9.2. Schematic illustration of the (Pa)g-barrel structure. The highly symmetrical structure presumably arose by multiple gene duplication events from a Pa-fragment. This hypothesis was tested using reverse engineering. Bisection of the barrel into two halves yielded correctly folded fragments which, upon heterodimerization, regained parental function. However, further fragmentation awaits experimental exploration.
RND is a large ubiquitous superfamiiy of transporters with representations in all domains of life. Composed typicahy of about 1000 amino-acid residues, they are arranged as 12 transmembrane hehces proteins with two large hydrophilic extra-cytoplasmic loops between hehces 1 and 2 and hehces 7 and 8. It has been postulated that these proteins developed from an internal gene duplication event. The members of the RND family are also secondary active transporters that catalyze the proton-motive-force driven transport of a range of substrates, including hydrophobic drugs, bile salts, fatty acids, heavy metals, and more (22). [Pg.364]

Construction of an evolutionary tree based on sequence comparisons revealed approximate times for the gene duplication events separating myoglobin and hemoglobin as well as the a and p subunits of hemoglobin. Evolutionary trees based on sequences can be compared to those based on fossil records. [Pg.297]

Isozymes differ in structural characteristics but catalyze the same reaction. They provide a means of fine-tuning metabolism to meet the needs of a given tissue or developmental stage. The results of gene-duplication events provide the means for subtle regulation of enzyme function. [Pg.443]

This reaction takes place in a second ATP-grasp domain within the enzyme. The active sites leading to carbamic acid formation and carbamoyl phosphate formation are very similar, revealing that this enzyme evolved by a gene duplication event. Indeed, duplication of a gene encoding an ATP-grasp domain followed by specialization was central to the evolution of nucleotide biosynthetic processes (Section 25.2.3). [Pg.1032]


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See also in sourсe #XX -- [ Pg.36 ]




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Duplicating events

Duplication

Gene duplication

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