P2 protamines from human sperm are zinc-finger proteins with one Cys2/His2 motif
P1 (HP1) and P2 (HP2, HP3, HP4) protamines were isolated from human sperm nuclei in the reduced form and their interaction with zinc and cobalt was studied. One zinc atom per molecule of P2 protamines but not of P1 protamine was found. Absorption spectra of P2 protamines with cobalt were characteris...
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Veröffentlicht in: | Biochemical and biophysical research communications 1992-01, Vol.182 (2), p.540-547 |
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creator | BIANCHI, F ROUSSEAUX-PREVOST, R SAUTIERE, P ROUSSEAUX, J |
description | P1 (HP1) and P2 (HP2, HP3, HP4) protamines were isolated from human sperm nuclei in the reduced form and their interaction with zinc and cobalt was studied. One zinc atom per molecule of P2 protamines but not of P1 protamine was found. Absorption spectra of P2 protamines with cobalt were characteristic of a tetrahedral complex involving two histidine and two cysteine residues and with one cobalt per molecule. A tetrahedral complex was found neither in P1 protamines nor in P2 protamines alkylated at cysteine or at histidine residues. The zinc finger motif Cys2/His2 of P2 protamines may play a role in stabilization of human sperm chromatin and in inhibition of transcription. |
doi_str_mv | 10.1016/0006-291X(92)91766-J |
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One zinc atom per molecule of P2 protamines but not of P1 protamine was found. Absorption spectra of P2 protamines with cobalt were characteristic of a tetrahedral complex involving two histidine and two cysteine residues and with one cobalt per molecule. A tetrahedral complex was found neither in P1 protamines nor in P2 protamines alkylated at cysteine or at histidine residues. The zinc finger motif Cys2/His2 of P2 protamines may play a role in stabilization of human sperm chromatin and in inhibition of transcription.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/0006-291X(92)91766-J</identifier><identifier>PMID: 1734868</identifier><identifier>CODEN: BBRCA9</identifier><language>eng</language><publisher>San Diego, CA: Elsevier</publisher><subject>Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Binding Sites ; Biological and medical sciences ; Chromatography, High Pressure Liquid ; Cystine - analysis ; Fundamental and applied biological sciences. 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One zinc atom per molecule of P2 protamines but not of P1 protamine was found. Absorption spectra of P2 protamines with cobalt were characteristic of a tetrahedral complex involving two histidine and two cysteine residues and with one cobalt per molecule. A tetrahedral complex was found neither in P1 protamines nor in P2 protamines alkylated at cysteine or at histidine residues. The zinc finger motif Cys2/His2 of P2 protamines may play a role in stabilization of human sperm chromatin and in inhibition of transcription.</description><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Cystine - analysis</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Histidine - analysis</subject><subject>Holoproteins</subject><subject>Humans</subject><subject>Male</subject><subject>Molecular Sequence Data</subject><subject>Nuclear proteins</subject><subject>Nuclear Proteins - isolation & purification</subject><subject>Protamines - chemistry</subject><subject>Protamines - isolation & purification</subject><subject>Proteins</subject><subject>Spectrophotometry, Atomic</subject><subject>Spectrophotometry, Ultraviolet</subject><subject>Spermatozoa - chemistry</subject><subject>Zinc - analysis</subject><subject>Zinc Fingers</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo90E9LwzAYBvAgypzTb6CQg4ge6vKnTZqjDHXKwB0UvJW3beIiTTqTFpmf3qrF03t4fjw8vAidUnJNCRVzQohImKKvl4pdKSqFSB730JQSRRJGSbqPpv_kEB3F-E4IpalQEzShkqe5yKdovWZ4G9oOnPU6YhNahze9A4_jVgeHIWj8ZX2VGOvfdPi12vqIP223wa3XeLGLbL60kWHXdtYcowMDTdQn452hl7vb58UyWT3dPyxuVsmW8axLpOCZyGvIgJemlFBXQnJCeFmbUmTZYDilINJaClYyTrMcuJBGKpKXKdPAZ-jir3dY9NHr2BXOxko3DXjd9rGQTCqZp-kAz0bYl07XxTZYB2FXjC8Y8vMxh1hBYwL4ysZ_llGV_-z5Bhvfafs</recordid><startdate>19920131</startdate><enddate>19920131</enddate><creator>BIANCHI, F</creator><creator>ROUSSEAUX-PREVOST, R</creator><creator>SAUTIERE, P</creator><creator>ROUSSEAUX, J</creator><general>Elsevier</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>19920131</creationdate><title>P2 protamines from human sperm are zinc-finger proteins with one Cys2/His2 motif</title><author>BIANCHI, F ; ROUSSEAUX-PREVOST, R ; SAUTIERE, P ; ROUSSEAUX, J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p235t-763568da5a3bfb7adc673003bdfb655235311a64d762b23158a367f7908b42ea3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Binding Sites</topic><topic>Biological and medical sciences</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Cystine - analysis</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Histidine - analysis</topic><topic>Holoproteins</topic><topic>Humans</topic><topic>Male</topic><topic>Molecular Sequence Data</topic><topic>Nuclear proteins</topic><topic>Nuclear Proteins - isolation & purification</topic><topic>Protamines - chemistry</topic><topic>Protamines - isolation & purification</topic><topic>Proteins</topic><topic>Spectrophotometry, Atomic</topic><topic>Spectrophotometry, Ultraviolet</topic><topic>Spermatozoa - chemistry</topic><topic>Zinc - analysis</topic><topic>Zinc Fingers</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>BIANCHI, F</creatorcontrib><creatorcontrib>ROUSSEAUX-PREVOST, R</creatorcontrib><creatorcontrib>SAUTIERE, P</creatorcontrib><creatorcontrib>ROUSSEAUX, J</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>BIANCHI, F</au><au>ROUSSEAUX-PREVOST, R</au><au>SAUTIERE, P</au><au>ROUSSEAUX, J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>P2 protamines from human sperm are zinc-finger proteins with one Cys2/His2 motif</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1992-01-31</date><risdate>1992</risdate><volume>182</volume><issue>2</issue><spage>540</spage><epage>547</epage><pages>540-547</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><coden>BBRCA9</coden><abstract>P1 (HP1) and P2 (HP2, HP3, HP4) protamines were isolated from human sperm nuclei in the reduced form and their interaction with zinc and cobalt was studied. One zinc atom per molecule of P2 protamines but not of P1 protamine was found. Absorption spectra of P2 protamines with cobalt were characteristic of a tetrahedral complex involving two histidine and two cysteine residues and with one cobalt per molecule. A tetrahedral complex was found neither in P1 protamines nor in P2 protamines alkylated at cysteine or at histidine residues. The zinc finger motif Cys2/His2 of P2 protamines may play a role in stabilization of human sperm chromatin and in inhibition of transcription.</abstract><cop>San Diego, CA</cop><pub>Elsevier</pub><pmid>1734868</pmid><doi>10.1016/0006-291X(92)91766-J</doi><tpages>8</tpages></addata></record> |
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subjects | Amino Acid Sequence Analytical, structural and metabolic biochemistry Binding Sites Biological and medical sciences Chromatography, High Pressure Liquid Cystine - analysis Fundamental and applied biological sciences. Psychology Histidine - analysis Holoproteins Humans Male Molecular Sequence Data Nuclear proteins Nuclear Proteins - isolation & purification Protamines - chemistry Protamines - isolation & purification Proteins Spectrophotometry, Atomic Spectrophotometry, Ultraviolet Spermatozoa - chemistry Zinc - analysis Zinc Fingers |
title | P2 protamines from human sperm are zinc-finger proteins with one Cys2/His2 motif |
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