Timirbulatova E R, Kireev I I, Kartavenko T V, Gulak P V, Poliakov V Iu, Guellec K L, Uzbekov R E
Research Institute of Physico-Chemical Biology, Moscow State University, Institute of Gene Biology RAS, Moscow.
Tsitologiia. 2003;45(3):290-7.
The interaction of condensin subunit XCAP-E with various nucleolar subcompartments in XL2 cells was studied. In the interphase cells, XCAP-E was associated with a granular component of nucleoli (as shown by double staining with antibodies against B23) and with small nucleolus-like structures in the nucleoplasm. Inhibition of transcription by actinomycin D does not disrupt interaction of XCAP-E with the granular compartment of segregated nucleoli. Treatment with DRB 5,6-dichloro-1 beta-ribofuranozide-benzimidazole causes disintegration of nucleolar fibrillar complexes, but does not affect nucleolar localization of XCAP-E. The data suggest that nucleolar association of XCAP-E is independent on the functional state of the nucleolus, and imply a possible role of this protein in rRNA processing and pre-fibosome assembly.
研究了凝聚素亚基XCAP-E与XL2细胞中各种核仁亚区室的相互作用。在间期细胞中，XCAP-E与核仁的颗粒成分相关（通过用抗B23抗体进行双重染色显示），并与核质中的小核仁样结构相关。放线菌素D抑制转录并不破坏XCAP-E与分离核仁的颗粒区室的相互作用。用DRB（5,6-二氯-1-β-核糖呋喃酰基-苯并咪唑）处理会导致核仁纤维复合体解体，但不影响XCAP-E在核仁中的定位。数据表明，XCAP-E与核仁的结合独立于核仁的功能状态，并暗示该蛋白在rRNA加工和前核糖体组装中可能发挥作用。
