Molecular Models of Acidic PePtides From Pea Bud Chromatin And Seminal Plasma. Divalent Cations-Mediated Interaction With Dna

Biological Chemistry - Tập 380 Số 1 - 1999
Loretta Mancinelli1, Francesco Chillemi, Elena Cardellini, Valeria Marsili, Flavio Giavarini, L. De Angelis, G Lugaro, G. Gianfranceschi
1Department of Cellular and Molecular Biology, University of Perugia, Italy

Tóm tắt

AbstractSmall acidic peptides have been isolated from biological fluids (blood and seminal plasma) and from chromatin of several tissues. Their biological activity is related to the control of cell growth and gene expression.This work is an approach to the study of peptide structure-function relationship. Purified fractions from seminal plasma and pea bud chromatin were subjected to fast ion bombardment mass spectrometry. The results obtained were analyzed according to biochemical characteristics of the peptides studied and some possible molecular models have been designed. Two of the proposed sequences were synthesized and their biological activity assayed in cells and cell-free systems. The results demonstrate that the synthetic peptides are able to bind to DNA in the presence of divalent cations (Mg

Từ khóa


Tài liệu tham khảo

10.1073/pnas.74.9.3869

10.1007/BF00776583

Andersen H.A., 1980, J. Cell. Sci., 45, 31, 10.1242/jcs.45.1.31

10.1007/BF00926836

Angiolillo A., 1993, by RNA polymerase II. Experientia, 49, 902

Bonfanti M., 1997, Cancer Res., 57, 1442

10.1016/0014-5793(91)81105-H

Coderoni S., 1988, from trout testis chromatin DNA. Physiol. Chem. Phys. Med. NMR, 20, 91

10.1016/0309-1651(84)90140-1

Fagioli M., 1992, Oncogene, 7, 1083

10.1002/(SICI)1099-1387(199701)3:1<54::AID-PSC68>3.0.CO;2-9

10.1038/262622a0

Gianfranceschi G.L., 1982, are bound to chromatin DNA. Biochim. Biophys. Acta, 699, 138

Gianfranceschi G.L., 1985, Progress in Non Histone Protein Research, I

Gianfranceschi G.L., 1989, Physiol. Chem. Phys. Med. NMR, 21, 289

10.1016/0196-9781(94)90163-5

10.1021/bi00172a006

Hillar M., 1979, Biochim. Biophys. Acta, 564, 246, 10.1016/0005-2787(79)90223-5

Hoffmann R., 1995, Int. J. Pept. Prot. Res., 45, 26, 10.1111/j.1399-3011.1995.tb01564.x

10.1021/ac970896z

10.1093/nar/19.23.6391

10.1074/jbc.270.24.14255

Lugaro G., 1988, Biochim. Biophys. Acta, 950, 420, 10.1016/0167-4781(88)90139-X

10.1038/344517a0

Mancinelli L., 1992, Physiol. Chem. Phys. Med. NMR, 24, 97

Manera E., 1984, IRCS Med. Sci., 12, 745

10.1007/BF00964553

10.3109/00207458408985594

10.1111/j.1471-4159.1984.tb06091.x

Marsili V., 1995, Cell. Mol. Biol., 41, 515

10.1139/cjpp-74-12-1302

Meek D.W., 1990, EMBO J., 9, 3253, 10.1002/j.1460-2075.1990.tb07524.x

Paulsen J.E., 1992, Cancer Res., 52, 1218

10.1016/0003-2697(89)90364-3

10.1021/jm960129c

10.1093/carcin/10.12.2249