Small peptides controlling transcription in vitro are bound to chromatin DNA

Gianfranceschi, G.; Barra, Donatella; Bossa, Francesco; Coderoni, S.; Paparelli, M; Venanzi, Franco; Cicconi, F.; Amici, Domenico

doi:10.1016/0167-4781(82)90147-6

Cited by 30 publications

(10 citation statements)

References 20 publications

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“…However, despite of repeated treatments with SDS / proteinase K and phenol, DNA isolated by this or similar procedures still contains residual proteinaceous material. For example, additional treatment with alkaline buffers releases another fraction of peptides [3] and even DNA isolated by prolonged cell lysis with strong alkali retains distinct polypeptides that are only released after degradation of the DNA [4]. These findings and other results indicating that chromosomal DNA contains structures becoming more alkali-sensitive after prolonged protease treatment [5,6] were regarded as indications for covalent bonds between (poly)peptides and nucleotides in chromosomal DNA.…”

Section: Introductionmentioning

confidence: 76%

Chemical and enzymatic analysis of covalent bonds between peptides and chromosomal DNA

Juodka¹,

Pfütz²,

Werner³

1991

Nucl Acids Res

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DNA from Ehrlich ascites tumor (EAT) cells and from human placenta was examined for covalent bonds between hydroxy amino acid residues in peptides and nucleotide phosphate groups. The residual proteinaceous material in highly purified DNA was radiolabelled with 125Iodine and the linking-groups between peptides and nucleotides released by combined protease and nuclease treatment were investigated with respect to their chemical and enzymatic stabilities. The residual nucleotide(s)-peptide(s) fraction from DNA isolated after prolonged alkaline cell lysis and phenol extraction contains mainly alkali and acid-stable but phosphodiesterase-sensitive peptide-nucleotide complexes which indicates phosphodiesters between tyrosyl residues in peptides and nucleotide phosphates. In contrast, the linking-group fraction from DNA isolated under native conditions contains additional peptide components. (a) Phospho-peptides that co-purify with DNA but that are not covalently bound to nucleotides. (b) A fraction of peptides that is released from nucleotides by alkali in a time and concentration-dependent reaction. Evidence is presented indicating that the latter fraction involves phospho-triesters between hydroxy amino acid residues in peptides and internucleotide phosphates. The phosphodiesters between hydroxy amino acids and nucleotide phosphates representing the predominant class of peptide-nucleotide complexes in alkali-denatured DNA are most likely side products of peptide-nucleotide phospho-triester hydrolysis.

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Section: Introductionmentioning

confidence: 76%

Chemical and enzymatic analysis of covalent bonds between peptides and chromosomal DNA

Juodka¹,

Pfütz²,

Werner³

1991

Nucl Acids Res

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“…Despite the difficulty represented by the presence of a family of closely related peptides and small amounts of purified peptides, some structural features have been demonstrated: (1) a molecular weight around 1000 dalton; (2) the presence of aspartic acid, serine, glutamic acid, glycine, alanine and valine in the acid hydrolysate [1,2]; (3) a blocked N-terminus consisting of pyroglutamic acid [1]; (4) a phosphoric group bound to serine side chain [6].…”

mentioning

confidence: 98%

“…Low molecular weight acidic peptides have been isolated both from bovine seminal plasma and from the chromatin of various tissues such as calf thymus, trout testis and bovine spermatozoa [1,2]. The isolated peptides act as regulators of RNA synthesis by exerting inhibitory effects on transcription in vitro and in neoplastic and fast-growing cells and an activating effect on senescent cells [3][4][5].…”

mentioning

confidence: 99%

Purification, Sequence Determination and Synthesis of Seminal Plasma Peptides and Synthesis of Some of Their Analogues

Francescato

Lugaro²,

Gianfranceschi

et al. 1997

J. Peptide Sci.

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Three peptides were isolated from bovine seminal plasma and purified to homogeneity. The amino acid sequences, as determined by FAB mass spectrometry, are the following: pGlu-Ala-Glu-Ser-Asn-OH, pGlu-Ala-Glu-Ser(PO3H2-Asn-OH and pGlu-Val-Gly-Glu-Ser-Glu-Asn-OH. These three peptides and some of their analogues were synthesized using liquid- and solid-phase techniques. The pentapeptide pGlu-Ala-Glu- Ser-Asn-OH showed a remarkable affinity for kinase NII and a strong inhibiting activity in DNA transcription. These findings support the hypothesis that phosphorylated acidic domains of nuclear non-histone proteins could bind to DNA, thereby controlling transcription.

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“…Even the most highly purified DNA has residual amino acids associated with it that can be detected by extraction with strong acids, bases, or other rigorous extraction procedures (1,2). These residual amino acids are thought to have been part of the original chromatin-scaffold proteins or other tightly bound chromatin proteins (2).…”

Section: Introductionmentioning

confidence: 99%

Complexing of amino acids to DNA by chromate in intact cells.

Voitkun

Zhitkovich

Costa

1994

Environ Health Perspect

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Using o-pthaldialdehyde (OPT) fluorescence, the amino acids associated with DNA were studied following exposure of intact Chinese hamster ovary cells to chromate. Rigorous extraction with EDTA, acid, or base was required to release the amino acids cross-linked to the DNA isolated from control or chromate-treated cells by standard procedures (i.e., proteinase K, phenol, etc.). Amino acids resisting extraction from DNA were not studied since analysis was limited to those that could be released by these procedures. There was a chromate dose-dependent increase in amino acids complexed with the DNA that could be released by EDTA, acid, and base, and these amino acids were separated by HPLC and identified. Substantial increases in cysteine, glutamine, glutamic acid, histidine, threonine, and tyrosine were found as a function of increasing concentrations of chromate. There was also a time-dependent increase in complexing of these amino acids to the DNA by chromate. The amino acids found complexed to DNA in intact cells by chromate were thought to originate from reactions of free amino acids or small peptides with the DNA rather than being proteolytic products derived from larger proteins that were cross-linked to the DNA. This was supported by a number of experiments: a) free amino acids or bovine serum albumin (BSA) were cross-linked by chromium to DNA in vitro and the DNA was isolated by standard procedures. With BSA, few amino acids were found cross-linked to the DNA, but with free amino acids, numerous amino acids were associated with DNA; b) when radiolabelled threonine complexed to the DNA was examined in the absence and presence of a protein synthesis inhibitor, there was substantial stimulation of the threonine complex to DNA by chromate when protein synthesis was inhibited with cyclohexamide; c) there were substantial increases in amino acids associated with DNA isolated without protease. Not only does the cross-linking of amino acids to DNA represent a new type of lesion to study in intact cells but it may also be a useful biomarker of human exposure to cross-linking agents. -Environ Health Perspect 102(Suppl 3): 251-255 (1994).

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Small peptides controlling transcription in vitro are bound to chromatin DNA

Cited by 30 publications

References 20 publications

Chemical and enzymatic analysis of covalent bonds between peptides and chromosomal DNA

Chemical and enzymatic analysis of covalent bonds between peptides and chromosomal DNA

Purification, Sequence Determination and Synthesis of Seminal Plasma Peptides and Synthesis of Some of Their Analogues

Complexing of amino acids to DNA by chromate in intact cells.

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