Antibodies specific for N 6‐methyladenosine react with intact snRNPs U2 and U4/U6

FEBS Letters

Lührmann, Reinhard¹  Bringmann, Peter¹ 

[1] Max-Planck-Institut für molekulare Genetik, Otto-Warburg-Laboratorium, D-1000 Berlin 33, Germany

关键词: U snRNP;    RNP structure;    Antibody;    Splicing;    N6-Methyladenosine;   

DOI  :  10.1016/0014-5793(87)81512-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Antibodies specific for N ⁶-methyladenosine (m⁶A) were elicited in rabbits and used to study the accessibility in intact snRNPs of the m⁶A residues present in the snRNAs U2, U4 and U6. The antibody quantitatively precipitates snRNPs U2 and U4/U6 from total nucleoplasmic snRNPs U1–U6 isolated from HeLa cells, which demonstrates that the m⁶A residues of the respective snRNAs are not protected by snRNP proteins in the snRNP particles. While the anti-m⁶A IgG does not react at all with U5 RNPs lacking m⁶A, a significant amount of U1 RNPs was co-precipitated despite the fact that U1 RNA does not contain m⁶A either. Since anti-m⁶A IgG does not react with purified U1 RNPs and co-precipitation of U1 RNPs is dependent on the presence of U2 RNPs but not of U4/U6 RNPs, these data indicate an interaction between snRNPs U1 and U2 in vitro. The anti-m⁶A precipitation pattern described above was also observed with snRNPs isolation from mouse Ehrlich ascites tumor cells, indicating similar three-dimensional arrangements of snRNAs in homologous snRNP particles from different organisms.

【 授权许可】

Unknown