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Elongin A (ELOA) is the transcriptionally active subunit of the heterotrimeric Elongin (also known as SIII) complex, composed of Elongin A (ELOA), Elongin B (ELOB), and Elongin C (ELOC)[1][2][3][4]. Elongin A stimulates the elongation phase of RNA polymerase II transcription by suppressing transient pausing and increasing the overall rate of transcript synthesis[1][3][4]. ELOA binds to the RPB2 subunit of Pol II, using specific domains—including a "latch" region that induces conformational changes near the polymerase’s active center, critical for its elongation-stimulatory activity[1][2]. In addition to its canonical role in transcription elongation, Elongin A participates in promoting Mediator complex loading during transcription initiation and can act as a substrate-recognition subunit in E3 ubiquitin ligases (via assembly with CUL5 and RBX2), directing ubiquitylation and proteasomal degradation of Pol II stalled at DNA lesions as part of the DNA damage response[1][3]. There are no approved drugs that directly target ELOA, and the protein does not serve as a common clinical biomarker[3]. However, dysregulation of the Elongin complex, including ELOA, is implicated in cancer, genome stability, and cellular stress responses[3].
Allosteric regulator of RNA polymerase II elongation; Adapter for E3 ubiquitin ligase complexes targeting Pol II
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