High mobility group 1 protein (HMG1) has traditionally been considered a structural component of chromatin, possibly similar in function to histone Hi. In fact, at the onset of Xenopus and Drosophila development, HMG1 appears to substitute for histone I-Il. HMG1 is abundant when histone H1 is absent after; the midblastula transition histone I-Il largely replaces HMG1. We show that in early mouse embryos the expression patterns of HMG1 and histone H1 are not complementary. Instead, HMG1 content increases after zygotic genome activation at the same time as histone H1. HMG1 does not remain associated to mitotic chromosomes either in embryos or somatic cells. These results argue against a shared structural role for HMG1 and histone H1 in mammalian chromatin. (C) 1998 Elsevier Science Ireland Ltd. All rights reserved.
High mobility group 1 (HMG1) protein in mouse preimplantation embryos
Bianchi, M E;
1998-01-01
Abstract
High mobility group 1 protein (HMG1) has traditionally been considered a structural component of chromatin, possibly similar in function to histone Hi. In fact, at the onset of Xenopus and Drosophila development, HMG1 appears to substitute for histone I-Il. HMG1 is abundant when histone H1 is absent after; the midblastula transition histone I-Il largely replaces HMG1. We show that in early mouse embryos the expression patterns of HMG1 and histone H1 are not complementary. Instead, HMG1 content increases after zygotic genome activation at the same time as histone H1. HMG1 does not remain associated to mitotic chromosomes either in embryos or somatic cells. These results argue against a shared structural role for HMG1 and histone H1 in mammalian chromatin. (C) 1998 Elsevier Science Ireland Ltd. All rights reserved.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
