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H1FOO Is Coupled to the Initiation of Oocytic Growth

Department of Obstetrics and Gynecology,² Keio University School of Medicine, Shinjuku-ku, Tokyo 160-0082, Japan Department of Obstetrics and Gynecology,³ Chiba University School of Medicine, Chuo-ku, Chiba 260-8670, Japan Division of Reproductive Sciences,⁴ Oregon National Primate Research Center, Oregon Health and Sciences University, Beaverton, Oregon 97006 The Jackson Laboratory,⁵ Bar Harbor, Maine 04609 Center for Animal Transgenesis and Germ Cell Research,⁶ University of Pennsylvania, School of Veterinary Medicine, Kennett Square, Pennsylvania 19348-1692 Division of Urology,⁷ Department of Surgery, University of Utah, School of Medicine, Salt Lake City, Utah 84132 Department of Gynecological Endocrinology,⁸ University of Medical Sciences in Poznan, 60-535 Poznan, Poland Developmental Endocrinology Branch,⁹ National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892 National Cancer Institute,¹⁰ NIH, Bethesda, Maryland 20892 Department of Biology,¹¹ University of Pennsylvania, Philadelphia, Pennsylvania 19104-6018 Division of Reproductive Sciences,¹² Huntsman Cancer Institute, University of Utah Health Sciences Center, Salt Lake City, Utah 84112

We previously reported the discovery of a novel mammalian H1 linker histone termed H1FOO (formerly H1OO), a replacement H1, the expression of which is restricted to the growing/ maturing oocyte and to the zygote. The significance of this pre-embryonic H1 draws on its substantial orthologous conservation, singular structural attributes, selectivity for the germ cell lineage, prolonged nucleosomal residence, and apparent predominance among germ cell H1s. Herein, we report that the intronic, single-copy, five-exon (5301 base pair) H1foo gene maps to chromosome 6 and that the corresponding primary H1foo transcript gives rise to two distinct, alternatively spliced mRNA species (H1foo and H1foo_ß). The expression of the oocytic H1FOO transcript and protein proved temporally coupled to the recruitment of resting primordial follicles into a developing primary follicular cohort and thus to the critical transition marking the onset of oocytic growth. The corresponding potential protein isoforms (H1FOO and H1FOO_ß), both nuclear localization sequence-endowed but export consensus sequence-free and possessing a significant net positive charge, localized primarily to perinucleolar heterochromatin in the oocytic germinal vesicle. Further investigation will be required to define the functional role of the H1FOO protein in the ordering of the chromatin of early mammalian development as well as its potential role in defining the primordial-to-primary follicle transition.

¹ Correspondence: Eli Y. Adashi, Division of Reproductive Sciences, University of Utah Health Sciences Center Huntsman Cancer Institute, 2000 Circle of Hope, Room 5221, Salt Lake City, UT 84112. FAX: 801 585 9256; eadashi{at}hsc.utah.edu

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