Sea Urchin Protease Specific to the SPKK Motif in Histone1

Suzuki, Masashi; Sugiura, Masayo; Ebashi, Setsuro

doi:10.1093/oxfordjournals.jbchem.a123205

Cited by 15 publications

(12 citation statements)

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“…This SPKK-protease differs from the SpH-cysteine protease not only in its biochemical properties, but most importantly, in its restricted specificity. As reported by Suzuki et al (1990), the SPKK protease promotes a limited proteolysis of only sperm histones H1 and H2B. Consequently, although the function of the SPKK-protease in the degradation of sperm histones during male pronucleus formation cannot be excluded, it would have a more limited role than that displayed by the SpHcysteine protease.…”

Section: Role Of Proteolysis In Chromatin Remodeling Of the Male Pronmentioning

confidence: 87%

“…Alternatively, a 28 kDa protease that specifically recognizes the SPKK motif in histones thereby cleaving at the potential phosphorylation target sites in SpH1 was also postulated to be involved in male pronuclei formation (Suzuki et al, 1990). This SPKK-protease differs from the SpH-cysteine protease not only in its biochemical properties, but most importantly, in its restricted specificity.…”

Section: Role Of Proteolysis In Chromatin Remodeling Of the Male Pronmentioning

confidence: 99%

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Chromatin remodeling during sea urchin early development: molecular determinants for pronuclei formation and transcriptional activation

Imschenetzky

Puchi

Morín

et al. 2003

Gene

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Section: Role Of Proteolysis In Chromatin Remodeling Of the Male Pronmentioning

confidence: 87%

Section: Role Of Proteolysis In Chromatin Remodeling Of the Male Pronmentioning

confidence: 99%

Chromatin remodeling during sea urchin early development: molecular determinants for pronuclei formation and transcriptional activation

Imschenetzky

Puchi

Morín

et al. 2003

Gene

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“…Another difference between the proteolytic activity described in the sea urchin and the one described in this work for H. tubulosa is its localization. While this activity is located inside the oocyte (cytoplasm) in the sea urchin (Suzuki et al . 1990; Imschenetzky et al .…”

Section: Discussionmentioning

confidence: 99%

“…There is evidence in literature that demonstrates that the sea urchin Paracentrotus lividus oocytes contain a proteolytic activity that is responsible for the in vitro differential degradation of the histones contained in the sperm nuclei of this species (Betzalel & Moav 1987). It has also been stated in several species of sea urchin that the oocyte contains a specific protease for the SPKK motif found in the spermatic histones SpH1 and SpH2B (Suzuki et al 1990). This SPKK protease has been purified as a 28 kDa monomer and its activity is inhibited by leupeptin, which acts upon the Ser-proteases (trypsinlike) and especially upon the Cys-proteases.…”

Section: Discussionmentioning

confidence: 99%

“…In the echinoderms group (Phylum Echinodermata), it has been described that the cytoplasm oocyte extracts from sea urchin (Class Echinoidea) contain a specific proteolytic activity against the SNBP (histones) (Betzalel & Moav 1987). A protease specific against the SPKK (Ser-Pro-basic-basic) motif of histones SpH1 and SpH2B has been identified in several sea urchin species and has been named SPKK protease (Suzuki et al 1990). In the sea urchin, it has been postulated that a complex mechanism of degradation/protection of the sperm specific histones during the chromatin remodeling transforms the sperm nucleus into the male pronucleus.…”

Section: Introductionmentioning

confidence: 99%

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In vitro decondensation of the sperm chromatin in Holothuria tubulosa (sea cucumber) not affecting proteolysis of basic nuclear proteins

Valle

2005

Dev Growth Differ

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Sea urchin and sea star oocyte extracts contain proteolytic activities that are active against sperm basic nuclear proteins (SNBP). This SNBP degradation has been related to the decondensation of sperm chromatin as a possible model to male pronuclei formation. We have studied the presence of this proteolytic activity in Holothuria tubulosa (sea cucumber) and its possible relationship with sperm nuclei decondensation. The mature oocyte extracts from H. tubulosa contain a proteolytic activity to SNBP located in the macromolecular fraction of the egg-jelly layer. SNBP degradation occurred both on sperm nuclei and on purified SNBP, histones being more easily degraded than protein Ø o (sperm-specific protein). SNBP degradation was found to be dependent on concentration, incubation time, presence of Ca 2+, pH, and this activity could be a serineproteinase. Thermal denaturalization of the oocyte extracts (80°C, 10-15 min) inactivates its proteolytic activity on SNBP but does not affect sperm nuclei decondensation. These results would suggest that sperm nuclei decondensation occurs by a mechanism different from SNBP degradation. Thus, the sperm nuclei decondensation occurs by a thermostable factor(s) and the removal of linker SNBP (H1 and protein Ø o ) will be a first condition in the process of sperm chromatin remodeling.

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Sea urchin sperm nuclear enlargement and shape transformations are differentially regulated in vitro

Raskin

Wright

1997

J. Exp. Zool.

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To elucidate the mechanisms regulating morphogenesis of the sperm nucleus into a male pronucleus after fertilization, we have used an in vitro cell‐free system derived from sea urchin eggs. Demembranated sperm nuclei were added to extracts prepared from either unfertilized eggs (unfertilized extract) or fertilized eggs (fertilized extract), and the area and shape of the sperm nuclei were measured using video‐intensified fluorescence microscopy coupled with image analysis. Sperm nuclei did not decondense in buffer used to prepare the extracts, indicating decondensation factors are of maternal origin. Unfertilized extract supported sperm nuclear decondensation to a greater extent than fertilized extract. This was not due to egg activation nor different preparation methods, but was due to the fertilizing sperm nucleus binding or inactivating diffusible decondensation factors within 10 min. Sperm nuclei needed constant exposure to egg cytoplasm for greater than 30 min for decondensation to proceed. Although sperm nuclear decondensation was temperature sensitive, a thermostable (100°C) decondensing factor was present in egg cytoplasm in limited quantities. Sperm nuclear decondensation was ATP‐dependent, pH‐sensitive, and required kinase activity, including tyrosine kinase activity. Shape transformations in fertilized extract were insensitive to 6‐dimethylaminopurine indicating the area and shape alterations are regulated differentially. In addition, alterations of shape, but not area, were sensitive to serine protease inhibitors, suggesting proteases change the sperm nuclear matrix, thereby altering shape. Sperm nuclear decondensation factors and their targets were highly conserved between sea urchin species, demonstrating a common decondensing mechanism is utilized, which may be applicable to other species. J. Exp. Zool. 277:401–416, 1997. © 1997 Wiley‐Liss, Inc.

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Sea Urchin Protease Specific to the SPKK Motif in Histone1

Cited by 15 publications

References 0 publications

Chromatin remodeling during sea urchin early development: molecular determinants for pronuclei formation and transcriptional activation

Chromatin remodeling during sea urchin early development: molecular determinants for pronuclei formation and transcriptional activation

In vitro decondensation of the sperm chromatin in Holothuria tubulosa (sea cucumber) not affecting proteolysis of basic nuclear proteins

Sea urchin sperm nuclear enlargement and shape transformations are differentially regulated in vitro

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