ArticleThe Journal of reproduction and development2015
Unique subcellular distribution of RPB1 with a phosphorylated C-terminal domain (CTD) in mouse oocytes during meiotic division and its relationship with chromosome separation.
Article in The Journal of reproduction and development, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed, 4 citations in OpenAlex.
- Natural degradation of RNA polymerase II is essential for oocyte chromatin reorganization and maternal-to-zygotic transition.Nature communications · 2025Article
- Expression ofAsian-Australasian journal of animal sciences · 2017Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Polymerase (RNA) II (DNA directed) polypeptide A (RPB1) is the largest subunit of RNA polymerase II (RNAPII), and phosphorylation of its C-terminal domain (CTD) is required for transcription initiation, elongation and RNA processing. Little is known about the CTD phosphorylation pattern and potential function during cell division when transcription is silenced. In this study, we assessed the protein expression and subcellular distribution of RPB1 during mouse oocyte meiotic division. Western blot analysis revealed that the RPB1 CTD was highly phosphorylated on Ser2 (pRPB1(Ser2)), Ser5 (pRPB1(Ser5)) and Ser7 (pRPB1(Ser7)). High and stable expression of pRPB1(Ser2) and pRPB1(Ser5) was detected from germinal vesicle (GV) to Metaphase II (MII) stage. In contrast, pRPB1(Ser7) only emerged after germinal vesicle breakdown (GVBD) and gradually increased to its peak level at metaphase I (MI) and MII. Immunofluorescence demonstrated that pRPB1(Ser2), pRPB1(Ser5) and pRPB1(Ser7) were pronouncedly aggregated within the nucleus of GV oocytes with a non-surrounded nucleolus (NSN) but very faintly labeled in oocytes with a surrounded nucleolus (SN). After meiotic resumption, pRPB1(Ser2) was again detected at spindle poles and co-localized with key microtubule organizing center (MTOC) components, pericentrin and γ-tubulin. pRPB1(Ser5) and pRPB1(Ser7) were assembled as filamentous aggregates and co-localized with microtubules throughout the spindle structure, responding to spindle-disturbing drugs, nocodazole or taxol, in pattern strongly similar to microtubules. pRPB1(Ser2) and pRPB1(Ser5) were constantly localized on chromosomes, with a relatively high concentration in centromere areas. Taken together, our data suggest that the CTD is highly phosphorylated and may be required for accurate chromosome segregation in mouse oocytes during meiosis.
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