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Heterochromatin Protein 1a (Hp1a) Partner Specificity Is Determined By Critical Amino Acids In The Chromo Shadow Domain And C-Terminal Extension, Deanna Lynn Mendez, Rebecca Mandt, Sarah C.R. Elgin
Heterochromatin Protein 1a (Hp1a) Partner Specificity Is Determined By Critical Amino Acids In The Chromo Shadow Domain And C-Terminal Extension, Deanna Lynn Mendez, Rebecca Mandt, Sarah C.R. Elgin
Biology Faculty Publications & Presentations
Drosophila melanogaster Heterochromatin Protein 1a (HP1a) is an essential protein critical for heterochromatin assembly and regulation. Its chromo shadow domain (CSD) homodimerizes, a requirement for binding protein partners that contain a PXVXL motif. How does HP1a select among its many different PXVXL-containing partners? HP1a binds tightly to Heterochromatin Protein 2 (HP2), but weakly to PIWI. We investigated differences in homodimerization and the impact of the C-terminal extension (CTE) by contrasting HP1a to its paralogue, HP1b. HP1a and HP1b differ in the dimerization interface, with HP1a having an Arg at position 188 rather than Glu. We find that while this substitution …