FEBS Letters | |
Association of the rat heterogeneous nuclear RNA‐ribonucleoprotein F with TATA‐binding protein | |
Yoshida, Tatsushi1  Tamura, Taka-aki2  Makino, Yasutaka1  | |
[1] Department of Biology, Faculty of Science, Chiba University, Chiba, Japan;CREST Japan Science and Technology Corporation, 1-33 Yayoicho, Inage-ku, Chiba 263-8522, Japan | |
关键词: Heterogeneous nuclear ribonucleoprotein F; Splicing factor; TATA-binding protein; Transcription factor; hnRNP-F; heterogeneous nuclear ribonucleoprotein F; TBP; TATA-binding protein; RNAP II; RNA polymerase II; CTD; carboxy-terminal domain; SDS-PAGE; SDS-polyacrylamide gel electrophoresis; PIC; pre-initiation complex; GTF; general transcription factor; HXmTBP; histidine-tagged mouse TBP; CPSF; cleavage-polyadenylation specificity factor; TIP; TBP-interacting protein; GST; glutathione S-transferase; PMSF; phenylmethylsulfonyl fluoride; | |
DOI : 10.1016/S0014-5793(99)01048-0 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Heterogeneous nuclear ribonucleoprotein F (hnRNP-F) has been shown to be a pre-mRNA splicing factor. Recent studies have uncovered the coordination of synthesis of pre-mRNA and its processing, including post-transcriptional modification and splicing. Here, we present evidence for an association between a splicing factor, hnRNP-F, and TATA-binding protein (TBP), which is an essential factor needed for transcription initiation. An affinity detection experiment revealed hnRNP-F in the preparation of TBP-interacting proteins. HnRNP-F was associated with TBP in nuclear extracts and was capable of direct binding to TBP in vitro. These results suggest that hnRNP-F is associated with TBP in the cell. HnRNP-F was observed in abundance in the thymus, spleen and testis, and its distribution pattern was similar to that of TBP, implying a functional coordination of transcription and splicing. We assume that the splicing machinery is associated with the transcription apparatus as a prerequisite prior to transcriptional elongation.
【 授权许可】
Unknown
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