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In molecular biology, SWI/SNF (SWItch/Sucrose Non-Fermentable), [1] [2] is a subfamily of ATP-dependent chromatin remodeling complexes, which is found in eukaryotes.In other words, it is a group of proteins that associate to remodel the way DNA is packaged.
In this case the recombination sites are slightly asymmetric, which allows the enzyme to tell apart the left and right ends of the site. When generating products, left ends are always joined to the right ends of their partner sites, and vice versa. This causes different recombination hybrid sites to be reconstituted in the recombination products.
Recombination can be artificially induced in laboratory (in vitro) settings, producing recombinant DNA for purposes including vaccine development. V(D)J recombination in organisms with an adaptive immune system is a type of site-specific genetic recombination that helps immune cells rapidly diversify to recognize and adapt to new pathogens.
Examples of bacterial species that have been found to possess multiple replicons include Rhodobacter sphaeroides (two), Vibrio cholerae, [3] and Burkholderia multivorans (three). These "secondary" (or tertiary) chromosomes are often described as molecules that are intermediate between a true chromosome and a plasmid and are sometimes called ...
The Eighth Day of Creation: Makers of the Revolution in Biology. Touchstone Books, ISBN 0-671-22540-5. 2nd edition: Cold Spring Harbor Laboratory Press, 1996 paperback: ISBN 0-87969-478-5. Micklas, David. 2003. DNA Science: A First Course. Cold Spring Harbor Press: ISBN 978-0-87969-636-8.
"Interaction of the Escherichia coli replication terminator protein (Tus) with DNA: a model derived from DNA-binding studies of mutant proteins by surface plasmon resonance."
The Rab family of proteins is a member of the Ras superfamily of small G proteins. [1] Approximately 70 types of Rabs have now been identified in humans. [2] Rab proteins generally possess a GTPase fold, which consists of a six-stranded beta sheet which is flanked by five alpha helices.
Pleckstrin homology domain (PH domain) or (PHIP) is a protein domain of approximately 120 amino acids that occurs in a wide range of proteins involved in intracellular signaling or as constituents of the cytoskeleton.