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Molecular architecture of the tRNA ligase complex

ABSTRACT: In human cells, a subset of tRNA-encoding genes contain introns. These are removed by a non-canonical splicing pathway in which the tRNA splicing endonuclease complex catalyzes intron excision and the resulting exons are subsequently ligated by the tRNA-ligase complex (tRNA-LC). The tRNA-LC is a hetero-pentameric protein assembly consisting of Ashwin, CGI-99, FAM98B, the DEAD-box helicase DDX1 and the catalytic subunit RTCB/HSPC117. We show that the paralogous proteins FAM98A and FAM98C underpin the assembly of compositionally distinct RTCB-containing complexes that lack Ashwin and may have distinct cellular functions.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Moritz Pfleiderer

LAB HEAD: Martin Jinek

PROVIDER: PXD068427 | Pride | 2026-08-04

REPOSITORIES: Pride

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			Action	DRS
	20230914_C32787_003_S558470_FAM98B_2_Group_2_DDA.raw	Raw
	20230914_C32787_004_S558466_FAM98A_1_Group_1_DDA.raw	Raw
	20230914_C32787_005_S558476_3xFLAG-mEGFP_2_Group_4_DDA.raw	Raw
	20230914_C32787_008_S558472_FAM98C_1_Group_3_DDA.raw	Raw
	20230914_C32787_009_S558475_3xFLAG-mEGFP_1_Group_4_DDA.raw	Raw

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