Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis最新文献

{"title":"A histone H4-specific methyltransferase","authors":"Peter Sarnow ,&nbsp;Ihab Rasched,&nbsp;Rolf Knippers","doi":"10.1016/0005-2787(81)90045-9","DOIUrl":"10.1016/0005-2787(81)90045-9","url":null,"abstract":"<div><p>A histone H4-specific methyltransferase was purified 80–100-fold from nuclei of calf lymphocytes and from calf thymus. Some biochemical properties of the enzyme are described. The enzyme transfers in vitro methyl groups from <span><math><mtext>S-</mtext><mtext>adenosylmethionine</mtext></math></span> preferentially to the lysine residue 20 of histone H4. This is the major in vivo methylation site of H4. DNA-bound or nucleosomal H4 is not methylated in vitro. We have used methylated and unmodified H4 (in the presence of sufficient quantities of the other core histones) for nucleosome reconstitution in vitro and have not found significant differences in the efficiencies of assembly.</p></div>","PeriodicalId":100164,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis","volume":"655 3","pages":"Pages 349-358"},"PeriodicalIF":0.0,"publicationDate":"1981-10-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2787(81)90045-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18297342","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"DNA methylase during Xenopus laevis development","authors":"R.L.P. Adams,&nbsp;R.H. Burdon,&nbsp;S. Gibb,&nbsp;E.L. McKay","doi":"10.1016/0005-2787(81)90042-3","DOIUrl":"10.1016/0005-2787(81)90042-3","url":null,"abstract":"<div><p>The DNA methylase activity present in embryos and cultured cells of <em>Xenopus laevis</em> resembles DNA methylase from mammalian tissues. Little or no activity is found in mature germinal vesicles, though nuclear activity rises rapidly after fertilization. This rise may result in part from a relocation of cytoplasmic enzyme.</p></div>","PeriodicalId":100164,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis","volume":"655 3","pages":"Pages 329-334"},"PeriodicalIF":0.0,"publicationDate":"1981-10-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2787(81)90042-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18297339","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Messenger RNA for ribosomal proteins in dormant and developing Artemia salina embryos","authors":"Paola Pierandrei-Amaldi,&nbsp;Nadia Campioni","doi":"10.1016/0005-2787(81)90046-0","DOIUrl":"10.1016/0005-2787(81)90046-0","url":null,"abstract":"<div><p>Ribosomal proteins from <em>Artemia salina</em> have been separated in a two-dimensional acrylamide gel system and assigned to the small and large ribosomal subunits. Poly(A)-containing RNA was prepared from dormant cysts and from polysomes of 30 min, 1 h, 5 h and 12 h embryos and hatching larvae. The mRNA from different stages was translated in a wheat-germ lysate and its template activity for ribosomal proteins was analyzed. It was observed that mRNA activity for ribosomal proteins is stored in the cytoplasm of dormant cysts and that it is found associated with polysomes of 30 min and of later stages.</p></div>","PeriodicalId":100164,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis","volume":"655 3","pages":"Pages 359-365"},"PeriodicalIF":0.0,"publicationDate":"1981-10-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2787(81)90046-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17234892","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Polynucleotide synthetase of E. coli: An enzyme complex having polynucleotide phosphorylase as apoenzyme","authors":"Jannis G. Stavrianopoulos ,&nbsp;Erwin Chargaff","doi":"10.1016/0005-2787(81)90040-X","DOIUrl":"10.1016/0005-2787(81)90040-X","url":null,"abstract":"<div><p>A previously described synthetase system of <em>Escherichia coli</em> that utilizes ribonucleoside triphosphates has been purified extensively and shown to consist of an apoenzyme and three protein factors. The apoenzyme itself was revealed to be polynucleotide phosphorylase. The conditions under which the latter — an enzyme incorporating nucleoside diphosphates — is converted to a system catalyzing the uptake of nucleoside triphosphates have been studied in detail with respect to primer requirements, the influence of triphosphates on diphosphate utilization and vice versa, and the possibly regulatory effect of the guanosine di- and triphosphates. The fully supplemented enzyme system (polynucleotide synthetase) incorporates GTP only in the presence of ATP, producing a polynucleotide with an A : G ratio near unity.</p></div>","PeriodicalId":100164,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis","volume":"655 3","pages":"Pages 307-322"},"PeriodicalIF":0.0,"publicationDate":"1981-10-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2787(81)90040-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18074097","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The modulating effect of isoproterenol on DNA replication and protein synthesis","authors":"James L Pipkin,&nbsp;William G Hinson,&nbsp;Jerry L Hudson,&nbsp;Jeanne Anson,&nbsp;L.Dave Pack","doi":"10.1016/0005-2787(81)90054-X","DOIUrl":"https://doi.org/10.1016/0005-2787(81)90054-X","url":null,"abstract":"<div><p>Within 96 h after initial isoproterenol administration, DNA replication and cell cycling were activated, as reflected in the bimodal distribution of nuclear fluorescence determined by flow-microfluorometric technques. A group of proteins, the cetyltrimethylammonium bromide extractable nuclear proteins (CTAB-proteins), isolated from electrostatically sorted nuclei of rat salivary glands, was shown by staining and autoradiography after two-dimensional electrophoresis to undergo differential synthesis during various phases of the in vivo cell cycle after isoproterenol administration. Stained chromatographs revealed quantitative differences in protein synthesis. Gel autoradiography was a more sensitive technique than staining for detecting nuclear protein synthesis during cell cycling. As observed in the autoradiographs of the CTAB-proteins, isoproterenol initiated two distinct periods of protein synthesis in the salivary gland cell cycle: one during the 2C population (G₀/G₁), and one during the 4C population (G₂/M). Protein synthesis after isoproterenol administration was much more dramatic in the 2C (isoproterenol) population, where 22 additional spots were observed, than in the 4C (isoproterenol) population, where five new spots were seen. There was less radioactive incorporation in the 4C (isoproterenol) population. Two spots ‘a’ and ‘b’ that demonstrate differential protein synthesis in stained gel chromatographs and gel autoradiographs were shown to have electrophoretic mobilities, molecular weights and amino acid compositions highly similar to those of HMG1 and HMG2, respectively. A positive correlation could also be drawn between quantitative levels of ‘a’ and ‘b’ and their levels of incorporation during cellular activity with HMG (high mobility group) proteins. For example protein ‘b’ (HMG2) was consistently more abundant in proliferating cell populations than in the quiescent ones. Autoradiographic patterns of the CTAB-proteins indicated that proteins ‘a’ and ‘b’ were synthesized during the <span><math><mtext>G</mtext><msub><mi></mi><mn>0</mn></msub><mtext>G</mtext><msub><mi></mi><mn>1</mn></msub></math></span> phase of the cell cycle, as were the majority of CTAB-proteins.</p></div>","PeriodicalId":100164,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis","volume":"655 3","pages":"Pages 421-431"},"PeriodicalIF":0.0,"publicationDate":"1981-10-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2787(81)90054-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"92001965","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Repair of ultraviolet-light-induced DNA damage in Vibrio cholerae","authors":"Goutam Das,&nbsp;Kaveri Sil,&nbsp;Jyotirmoy Das","doi":"10.1016/0005-2787(81)90053-8","DOIUrl":"10.1016/0005-2787(81)90053-8","url":null,"abstract":"<div><p>Repair of ultraviolet-light-induced DNA damage in a highly pathogenic Gram-negative bacterium, <em>Vibrio cholerae</em>, has been examined. All three strains of <em>V. cholerae</em> belonging to two serotypes, Inaba and Ogawa, are very sensitive to ultraviolet irradiation, having inactivation cross-sections ranging from 0.18 to 0.24 m²/J. Although these cells are proficient in repairing the DNA damage by a photoreactivation mechanism, they do not possess efficient dark repair systems. The mild toxinogenic strain 154 of classical <em>Vibrios</em> presumably lacks any excision repair mechanism and studies of irradiated cell DNA indicate that the ultraviolet-induced pyrimidine dimers may not be excised. Ultraviolet-irradiated cells after saturation of dark repair can be further photoreactivated.</p></div>","PeriodicalId":100164,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis","volume":"655 3","pages":"Pages 413-420"},"PeriodicalIF":0.0,"publicationDate":"1981-10-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2787(81)90053-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18297300","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Heterogeneity of neutral ribonuclease II and ribonuclease II-inhibitor complex from mouse skeletal muscle","authors":"B.W. Little,&nbsp;L.S. Whittingham","doi":"10.1016/0005-2787(81)90015-0","DOIUrl":"10.1016/0005-2787(81)90015-0","url":null,"abstract":"<div><p>Using either DEAE-cellulose chromatography or pH 4–6 isoelectric focusing, we have separated mouse skeletal muscle neutral RNAase II-inhibitor complex into two fractions (designated α and β).<em>para</em>-Hydroxymercuriphenylsulfonate-induced dissociation/inactivation of the inhibitor yields free RNAase II enzyme fractions with differing pH profiles, CM-cellulose chromatographic behavior and reactivity with the RNAase II inhibitor of human placenta. However, the free RNAase fractions react equally with purified inhibitor from skeletal muscle and are not separable by pH 8–9.5 isoelectric focusing. These data suggest that mouse skeletal muscle has two heterogeneous forms of RNAase II. Additionally, heterologous RNAase II inhibitors may be used as investigational tools when probing neutral RNAase II heterogeneity.</p></div>","PeriodicalId":100164,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis","volume":"655 2","pages":"Pages 251-255"},"PeriodicalIF":0.0,"publicationDate":"1981-09-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2787(81)90015-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17332659","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Complete assignment and conformational analysis of a deoxyribotetranucleotide, d(TAAT). A 360 and 500 MHz NMR study","authors":"Jan-Remt Mellema,&nbsp;Cornelis A.G. Haasnoot ,&nbsp;Jacques H. Van Boom,&nbsp;Cornelis Altona","doi":"10.1016/0005-2787(81)90016-2","DOIUrl":"10.1016/0005-2787(81)90016-2","url":null,"abstract":"<div><p>A proton NMR study at 360 MHz and 500 MHz was carried out on the tetranucleoside triphosphate d(TAAT) at a temperature of 27°C. Extensive decoupling experiments allowed a complete and unambiguous spectral assignment. The data are interpreted in terms of the N and S deoxyribose pseudorotational ranges. From the observed proton-proton coupling constants it is calculated that (a) the populations of deoxyribose S-form are as follows: dT(1)-, 85%; -dA(2)-, 97%; -dA(3)-, 81%; -dT(4), 64%; and (b) the g⁺ populations (backbone notation) along the exocyclic C4′-C5′ bond in -dA(2)-, dA(3)- and -dT(4) are 82%, 86% and 78%, respectively. From these values, combined with chemical shift considerations, it is concluded that the central -dA(2)-dA(3)- part of the molecule occurs preferentially as a mixture of two right-handed single-helical conformations, denoted S-S and S-N, in a ratio of approximately 8 : 2. This situation closely mimics that found for the 3′-end of d(A-A-A) (Olsthoorn, C.S.M., Bostelaar, L.J., Van Boom, J.H. and Altona, C. (1980) Eur. J. Biochem. 112, 95–110). Similarly, the conformational behaviour of the dT(1)-dA(2)- and -dA(3)-dT(4) terminals appears roughly identical to that displayed by the corresponding dinucleoside monophosphates. The molecule as a whole does not show signs of cooperativity of stacking.</p></div>","PeriodicalId":100164,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis","volume":"655 2","pages":"Pages 256-264"},"PeriodicalIF":0.0,"publicationDate":"1981-09-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2787(81)90016-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18297336","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Template-binding site of AMV reverse transcriptase and inactivation of the enzyme by N-ethylmaleimide","authors":"Veena K. Parnaik,&nbsp;M.R. Das","doi":"10.1016/0005-2787(81)90007-1","DOIUrl":"10.1016/0005-2787(81)90007-1","url":null,"abstract":"<div><p><span><math><mtext>N-</mtext><mtext>Ethylmaleimide</mtext></math></span>, a sulfhydryl-specific reagent, strongly inhibits AMV reverse transcriptase by specifically interfering with the template-binding site of the enzyme. However, the kinetics of inhibition differ widely with the composition and structure of the templates employed. The copying of templates with multiple 3′-hydroxyl termini appeared to be more susceptible to <span><math><mtext>N-</mtext><mtext>ethylmaleimide</mtext></math></span> treatment, suggesting that the reagent may interfere with initiation of DNA synthesis. The ability of a template bound to enzyme prior to <span><math><mtext>N-</mtext><mtext>ethylmaleimide</mtext></math></span> treatment to protect against inactivation of copying of other templates also, implies a common binding site for the different templates. Template exchange experiments demonstrated competition between activated calf thymus DNA and rA_n · dT_12–18 for binding to the enzyme. Thus, templates varying widely in composition and conformation appear to bind at a common site on reverse transcriptase. The experimental data also show suggestive evidence for small but finite differences in the requirements for optimal binding for templates of different structures.</p></div>","PeriodicalId":100164,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis","volume":"655 2","pages":"Pages 181-188"},"PeriodicalIF":0.0,"publicationDate":"1981-09-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2787(81)90007-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17234891","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Protection of rat liver 80 S ribosomes against ricin A chain inactivation by proteins extracted from rat liver and wheat germ ribosomal subunits with ammonium chloridemagnesium chloride","authors":"Ming-Shi Chang,&nbsp;L.L Houston","doi":"10.1016/0005-2787(81)90013-7","DOIUrl":"10.1016/0005-2787(81)90013-7","url":null,"abstract":"<div><p>Proteins extracted from wheat germ 60 S ribosomal subunits and rat liver 60 S and 40 S ribosomal subunits with <span><math><mtext>3 </mtext><mtext>M NH</mtext><msub><mi></mi><mn>4</mn></msub><mtext>Cl</mtext><mtext>75 </mtext><mtext>mM MgCl</mtext><msub><mi></mi><mn>2</mn></msub></math></span> were able to prevent the ricin A chain-mediated inactivation of untreated 80 S rat liver ribosomes. The protection of polyphenylalanine synthetic capability of 80 S ribosomes was saturable and reached 100% protection in the presence of about 20 μg of extracted protein using a uniform set of assay conditions. No protection was observed using proteins extracted from wheat germ 40 S subunits or the core fraction of rat liver 60 S subunits or protein extracted from <em>Escherichia coli</em> ribosomes or ribosomal subunits. The conclusion that the protective effect of extracted 60 S subunit proteins was specific, was further strengthened by showing that unrelated proteins such as α-lactalbumin, bovine serum albumin and lysozyme, and polypeptides such as polylysine and poly(aspartic acid), also showed no protection. If 80 S ribosomes were first treated with ricin A chain and then incubated with proteins extracted from rat liver 60 S subunits, no protection was observed. Proteins extracted with <span><math><mtext>NH</mtext><msub><mi></mi><mn>4</mn></msub><mtext>Cl</mtext><mtext>MgCl</mtext><msub><mi></mi><mn>2</mn></msub></math></span> from 60 S rat liver subunits were applied to a carboxymethylcellulose column equilibrated with 6 M urea. Stepwise elution with increasing concentrations of LiCl resulted in seven fractions. One fraction (D) contained most of the protective factor; one fraction (E) contained a lesser amount of the protective factor. Two-dimensional polyacrylamide gel electrophoresis of fraction D showed the presence of ten proteins. These data are consistent with the idea that the enzymatic target of ricin A chain is protein is nature and that fraction D contains one or more proteins that appear to act as a inhibitor against ricin A chain.</p></div>","PeriodicalId":100164,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis","volume":"655 2","pages":"Pages 230-242"},"PeriodicalIF":0.0,"publicationDate":"1981-09-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2787(81)90013-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18298401","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}