M‐phase‐specific histone H1 kinase in fish oocytes: Purification, components and biochemical properties

Masakane YAMASHITA, Sachiko FUKADA, Michiyasu Yoshikuni, Philippe BULET, Toshiaki HIRAI, Akihiko Yamaguchi, Hideyo YASUDA, Yoshiki OHBA, Yoshitaka NAGAHAMA

研究成果: ジャーナルへの寄稿記事

59 引用 (Scopus)

抄録

We demonstrate, for the first time in fish, that a Ca2+‐independent and cyclic‐nucleotide‐independent histone H1 kinase activity oscillates according to the cell cycle of the oocyte, peaking at the first and the second meiotic metaphase with a transient drop between them. The kinase, M‐phase‐specific histone H1 kinase (M‐H1K), was purified from mature carp oocytes by using two exogenous substrates for assaying its activity: histone H1 and a synthetic peptide (SP peptide, KKAAKSPKKAKK) containing the sequence KSPKK, which includes the consensus sequence of the site phosphorylated by a serine/threonine‐specific protein kinase encoded by the fission yeast cdc2+ gene (cdc2 kinase). The M‐H1K and maturation‐promoting factor (MPF) activities coincided closely throughout four steps of purification, strongly suggesting the identity of M‐H1K and MPF. The final preparation was purified 5000‐fold with a recovery of 4%, when histone H1 was used for the kinase assay, and 10000‐fold with a recovery of 7% when SP peptide was used. The purified molecular mass of the kinase was estimated to be 100 kDa by gel filtration and contained four proteins of 33,34,46 and 48 kDa. Anti‐PSTAIR antibody recognizing cdc2 kinase cross‐reacted with the 33‐kDa and 34‐kDa proteins, while the 46‐kDa and 48‐kDa bands cross‐reacted with monoclonal antibodies raised against cyclin B. The 33‐kDa protein was also recognized by an antibody against a goldfish cdk2 (Eg1) kinase, a cdc2‐related kinase which has the PSTAIR sequence and binds to p13suc1 but does not form a complex with cyclin B. M‐H1K activity corresponded well to the 34‐kDa, 46‐kDa and 48‐kDa proteins but not to the 33‐kDa protein. These results strongly suggest that M‐H1K consists of cdc2 kinase forming a complex with cyclin B, and that cdk2 kinase is not a component of M‐H1K, although it is found in the highly purified M‐H1K. The purified M‐H1K utilized Mg2+, Mn2+, ATP and GTP, and had a wide pH optimum ranging over 8.0–10.5. The kinase was thermolabile and sensitive to freezing/thawing.

元の言語英語
ページ(範囲)537-543
ページ数7
ジャーナルEuropean Journal of Biochemistry
205
発行部数2
DOI
出版物ステータス出版済み - 1 1 1992

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Fish
Oocytes
Purification
Fishes
Phosphotransferases
Cyclin B
Proteins
Histones
Peptides
histone H1 kinase
Recovery
Thawing
Antibodies
Protein-Serine-Threonine Kinases
Goldfish
Molecular mass
Carps
Schizosaccharomyces
Guanosine Triphosphate
Consensus Sequence

All Science Journal Classification (ASJC) codes

  • Biochemistry

これを引用

M‐phase‐specific histone H1 kinase in fish oocytes : Purification, components and biochemical properties. / YAMASHITA, Masakane; FUKADA, Sachiko; Yoshikuni, Michiyasu; BULET, Philippe; HIRAI, Toshiaki; Yamaguchi, Akihiko; YASUDA, Hideyo; OHBA, Yoshiki; NAGAHAMA, Yoshitaka.

:: European Journal of Biochemistry, 巻 205, 番号 2, 01.01.1992, p. 537-543.

研究成果: ジャーナルへの寄稿記事

YAMASHITA, Masakane ; FUKADA, Sachiko ; Yoshikuni, Michiyasu ; BULET, Philippe ; HIRAI, Toshiaki ; Yamaguchi, Akihiko ; YASUDA, Hideyo ; OHBA, Yoshiki ; NAGAHAMA, Yoshitaka. / M‐phase‐specific histone H1 kinase in fish oocytes : Purification, components and biochemical properties. :: European Journal of Biochemistry. 1992 ; 巻 205, 番号 2. pp. 537-543.
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abstract = "We demonstrate, for the first time in fish, that a Ca2+‐independent and cyclic‐nucleotide‐independent histone H1 kinase activity oscillates according to the cell cycle of the oocyte, peaking at the first and the second meiotic metaphase with a transient drop between them. The kinase, M‐phase‐specific histone H1 kinase (M‐H1K), was purified from mature carp oocytes by using two exogenous substrates for assaying its activity: histone H1 and a synthetic peptide (SP peptide, KKAAKSPKKAKK) containing the sequence KSPKK, which includes the consensus sequence of the site phosphorylated by a serine/threonine‐specific protein kinase encoded by the fission yeast cdc2+ gene (cdc2 kinase). The M‐H1K and maturation‐promoting factor (MPF) activities coincided closely throughout four steps of purification, strongly suggesting the identity of M‐H1K and MPF. The final preparation was purified 5000‐fold with a recovery of 4{\%}, when histone H1 was used for the kinase assay, and 10000‐fold with a recovery of 7{\%} when SP peptide was used. The purified molecular mass of the kinase was estimated to be 100 kDa by gel filtration and contained four proteins of 33,34,46 and 48 kDa. Anti‐PSTAIR antibody recognizing cdc2 kinase cross‐reacted with the 33‐kDa and 34‐kDa proteins, while the 46‐kDa and 48‐kDa bands cross‐reacted with monoclonal antibodies raised against cyclin B. The 33‐kDa protein was also recognized by an antibody against a goldfish cdk2 (Eg1) kinase, a cdc2‐related kinase which has the PSTAIR sequence and binds to p13suc1 but does not form a complex with cyclin B. M‐H1K activity corresponded well to the 34‐kDa, 46‐kDa and 48‐kDa proteins but not to the 33‐kDa protein. These results strongly suggest that M‐H1K consists of cdc2 kinase forming a complex with cyclin B, and that cdk2 kinase is not a component of M‐H1K, although it is found in the highly purified M‐H1K. The purified M‐H1K utilized Mg2+, Mn2+, ATP and GTP, and had a wide pH optimum ranging over 8.0–10.5. The kinase was thermolabile and sensitive to freezing/thawing.",
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T1 - M‐phase‐specific histone H1 kinase in fish oocytes

T2 - Purification, components and biochemical properties

AU - YAMASHITA, Masakane

AU - FUKADA, Sachiko

AU - Yoshikuni, Michiyasu

AU - BULET, Philippe

AU - HIRAI, Toshiaki

AU - Yamaguchi, Akihiko

AU - YASUDA, Hideyo

AU - OHBA, Yoshiki

AU - NAGAHAMA, Yoshitaka

PY - 1992/1/1

Y1 - 1992/1/1

N2 - We demonstrate, for the first time in fish, that a Ca2+‐independent and cyclic‐nucleotide‐independent histone H1 kinase activity oscillates according to the cell cycle of the oocyte, peaking at the first and the second meiotic metaphase with a transient drop between them. The kinase, M‐phase‐specific histone H1 kinase (M‐H1K), was purified from mature carp oocytes by using two exogenous substrates for assaying its activity: histone H1 and a synthetic peptide (SP peptide, KKAAKSPKKAKK) containing the sequence KSPKK, which includes the consensus sequence of the site phosphorylated by a serine/threonine‐specific protein kinase encoded by the fission yeast cdc2+ gene (cdc2 kinase). The M‐H1K and maturation‐promoting factor (MPF) activities coincided closely throughout four steps of purification, strongly suggesting the identity of M‐H1K and MPF. The final preparation was purified 5000‐fold with a recovery of 4%, when histone H1 was used for the kinase assay, and 10000‐fold with a recovery of 7% when SP peptide was used. The purified molecular mass of the kinase was estimated to be 100 kDa by gel filtration and contained four proteins of 33,34,46 and 48 kDa. Anti‐PSTAIR antibody recognizing cdc2 kinase cross‐reacted with the 33‐kDa and 34‐kDa proteins, while the 46‐kDa and 48‐kDa bands cross‐reacted with monoclonal antibodies raised against cyclin B. The 33‐kDa protein was also recognized by an antibody against a goldfish cdk2 (Eg1) kinase, a cdc2‐related kinase which has the PSTAIR sequence and binds to p13suc1 but does not form a complex with cyclin B. M‐H1K activity corresponded well to the 34‐kDa, 46‐kDa and 48‐kDa proteins but not to the 33‐kDa protein. These results strongly suggest that M‐H1K consists of cdc2 kinase forming a complex with cyclin B, and that cdk2 kinase is not a component of M‐H1K, although it is found in the highly purified M‐H1K. The purified M‐H1K utilized Mg2+, Mn2+, ATP and GTP, and had a wide pH optimum ranging over 8.0–10.5. The kinase was thermolabile and sensitive to freezing/thawing.

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