Histone phosphorylation during sea urchin development

Green, G.R.; Collas, Philippe; Burrell, Allison S.; Poccia, Dominic

doi:10.1006/scel.1995.0030

Cited by 23 publications

(15 citation statements)

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“…Sperm chromatin decondensation has been shown to be accompanied by changes in sperm histone phosphorylation (28,29).…”

Section: Methodsmentioning

confidence: 99%

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Protein Kinase C-mediated Interphase Lamin B Phosphorylation and Solubilization

Collas¹,

Thompson²,

Fields³

et al. 1997

Journal of Biological Chemistry

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Disassembly of the sperm nuclear envelope at fertilization is one of the earliest events in the development of the male pronucleus. We report that nuclear lamina disassembly in interphase sea urchin egg cytosol is a result of lamin B phosphorylation mediated by protein kinase C (PKC). Lamin B of permeabilized sea urchin sperm nuclei incubated in fertilized egg G 1 phase cytosolic extract is phosphorylated within 1 min of incubation and solubilized prior to sperm chromatin decondensation. Phosphorylation is Ca 2؉ -dependent. It is reversibly inhibited by the PKC-specific inhibitor chelerythrine, a PKC pseudosubstrate inhibitor peptide, and a PKC substrate peptide, but not by inhibitors of PKA, p34 cdc2 or calmodulin kinase II. Phosphorylation is inhibited by immunodepletion of cytosolic PKC and restored by addition of purified rat brain PKC. Sperm lamin B is a substrate for rat brain PKC in vitro, resulting in lamin B solubilization. Two-dimensional phosphopeptide maps of lamin B phosphorylated by the cytosolic kinase and by purified rat PKC are virtually identical. These data suggest that PKC is the major kinase required for interphase disassembly of the sperm lamina.The nuclear lamina consists of a polymeric network of intermediate filament molecules, the nuclear lamins, underlying the inner nuclear membrane. The lamina is a dynamic structure, undergoing expansion during interphase of the cell cycle, and depolymerization at mitosis upon breakdown of the nuclear envelope (NE) 1 (1). Mitotic disassembly and reassembly of the lamina is regulated by reversible lamin phosphorylation and dephosphorylation (1). Interphase lamin phosphorylation has also been reported (2-6), but its significance is not fully understood.Several lamin kinases have been identified that promote mitotic lamina solubilization or inhibit lamina assembly in vitro. They include cyclin B/p34 cdc2 (7), S6 kinase II (8), protein kinase C (PKC) (4, 9), and the cAMP-dependent protein kinase PKA (10). Down-regulation of PKA has also been shown to be essential for mitotic lamina disassembly (11). Although not a lamin kinase, Ca 2ϩ /calmodulin-dependent kinase II (CaM kinase II) is also involved in mitotic NE breakdown in sea urchin embryos (12). PKC has also been shown to phosphorylate chicken lamin B 2 in interphase, a process thought to regulate lamin import into the nucleus (13). These observations imply that multiple kinases regulate the dynamics of the nuclear lamina during the cell cycle. The transformation of the sea urchin sperm nucleus into a pronucleus at fertilization provides an opportunity to investigate NE assembly/disassembly during interphase. Sea urchin eggs are fertilized in G 1 phase of the first cell cycle after completion of both meiotic divisions. At fertilization, the sperm NE vesiculates and a new NE reforms around the male pronucleus as the sperm chromatin decondenses (14). Male pronuclear formation has been duplicated in a cell-free system by incubating detergent-permeabilized sperm nuclei in fertilized egg extracts (15)(16)(1...

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“…Sperm chromatin decondensation has been shown to be accompanied by changes in sperm histone phosphorylation (28,29).…”

Section: Methodsmentioning

confidence: 99%

“…Sperm histones SpH1 and SpH2B are phosphorylated in vivo within 3 min of fertilization (43), as well as in vitro, albeit at a slower rate (29). Interestingly, the conversion of Sp histones to their modified form in vivo takes place in eggs treated with DMAP, indicating that the sperm histone kinase is DMAPinsensitive (41).…”

Section: Pkc-mediated Interphase Laminmentioning

confidence: 99%

Protein Kinase C-mediated Interphase Lamin B Phosphorylation and Solubilization

Collas¹,

Thompson²,

Fields³

et al. 1997

Journal of Biological Chemistry

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“…The same appears to be true for the variants, since histone H1 variants are phosphorylated on their tails during deposition into chromatin and prior to their removal from chromatin (Wagner et al 1977;Poccia and Green 1992;Green et al 1995;Dou et al 1999). …”

Section: H1 Modificationsmentioning

confidence: 97%

“…The few that have been documented completely replace the major H2B subtypes and appear to have very specialized functions in chromatin compaction and transcription re- pression, particularly during gametogenesis (for review, see Poccia and Green 1992;Green et al 1995). Unlike the major H2B subtypes, the sperm-specific H2B in sea urchins has a long N-terminal tail that is highly charged.…”

Section: Histone H2bmentioning

confidence: 99%

Histone variants: deviants?

Kamakaka

Biggins²

2005

Genes Dev.

319

263

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Histones are a major component of chromatin, the protein-DNA complex fundamental to genome packaging, function, and regulation. A fraction of histones are nonallelic variants that have specific expression, localization, and species-distribution patterns. Here we discuss recent progress in understanding how histone variants lead to changes in chromatin structure and dynamics to carry out specific functions. In addition, we review histone variant assembly into chromatin, the structure of the variant chromatin, and post-translational modifications that occur on the variants.

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“…Sperm nuclei incubated in sea urchin egg extract display phosphorylation of Sp H1 and Sp H2B (Green et al, 1995). In addition, small amounts of CS H1 appear in these nuclei, but CS H1 does not accumulate in vitro to levels detected in male pronuclei in vivo.…”

Section: Phosphorylation Of Sperm Histonesmentioning

confidence: 96%