Oligo(3'‐deoxyADP‐ribosyl)ation of thenuclear matrix lamins from rat liver utilizing 3'‐deoxyNAD as a substrate

FEBS Letters

Alvarez-Gonzalez, Rafael¹  Pedraza-Reyes, Mario¹ 

[1] Department of Microbiology and Immunology, Texas College of Osteopathic Medicine, 3500 Camp Bowie Boulevard, Fort Worth, TX 76107-2690, USA

关键词: 3'-DeoxyNAD;    Lamin;    Nuclear matrix;    LiDS-PAGE;    Poly(ADP-ribose)polymerase;    Rat liver;   

DOI  :  10.1016/0014-5793(90)80815-Z

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

It has previously been shown that the levels of poly(ADP-ribose)polymerase and polymers of ADP-ribose that co-purify with the nuclear matrix in regenerating liver fluctuate with the levels of in vivo DNA replication [(1988) FEBS Lett. 236, 362-366]. We have now electrophoretically identified lamins A and C, and poly(ADP-ribose)polymerase as the main protein targets for poly(ADP-ribosyl)ation in isolated nuclear matrices from adult rat liver. The identification of these protein acceptors was facilitated by the utilization of ³²P-radiolabeled 3'-deoxyNAD as a substrate for nuclear matrix extracts in the presence of exogenously added DNA-dependent poly(ADP-ribose)polymerase from calf thymus. The extent of protein modification was time- and substrate concentration-dependent. These results are consistent with the hypothesis that the poly(ADP-ribose) modification of the lamins A and C and poly(ADP-ribose)polymerase are important to modulate chromatin-nuclear matrix interactions in rat liver.

【 授权许可】

Unknown