Proto-oncoprotein TLS/FUS is associated to the nuclear matrix and complexed with splicing factors PTB, SRm160, and SR proteins
M Meissner, S Lopato, J Gotzmann… - Experimental cell …, 2003 - Elsevier
M Meissner, S Lopato, J Gotzmann, G Sauermann, A Barta
Experimental cell research, 2003•ElsevierTLS/FUS is a nucleic acid-binding protein whose N-terminal half functions as a
transcriptional activator domain in fusion oncoproteins found in human leukemias and
liposarcomas. Previous reports have suggested a role for TLS/FUS in transcription and
splicing processes. Here we report the association of TLS/FUS with the nuclear matrix and
investigate its role in splicing. Splicing of two pre-mRNAs was inhibited in a TLS/FUS-
immunodepleted extract and could only be partly restored by addition of recombinant …
transcriptional activator domain in fusion oncoproteins found in human leukemias and
liposarcomas. Previous reports have suggested a role for TLS/FUS in transcription and
splicing processes. Here we report the association of TLS/FUS with the nuclear matrix and
investigate its role in splicing. Splicing of two pre-mRNAs was inhibited in a TLS/FUS-
immunodepleted extract and could only be partly restored by addition of recombinant …
TLS/FUS is a nucleic acid-binding protein whose N-terminal half functions as a transcriptional activator domain in fusion oncoproteins found in human leukemias and liposarcomas. Previous reports have suggested a role for TLS/FUS in transcription and splicing processes. Here we report the association of TLS/FUS with the nuclear matrix and investigate its role in splicing. Splicing of two pre-mRNAs was inhibited in a TLS/FUS-immunodepleted extract and could only be partly restored by addition of recombinant TLS/FUS or/and SR proteins, known interaction partners of TLS/FUS. The subsequent analysis of TLS/FUS immunoprecipitates revealed that, in addition to the SR proteins SC35 and SRp75, the splicing factor PTB (hnRNPI) and the splicing coactivator SRm160 are complexed with TLS/FUS, thus explaining the inability to restore splicing completely. Coimmunolocalization confirmed the nuclear matrix association and interaction of TLS/FUS with PTB, SR proteins, and SRm160. Our results suggest that the matrix protein TLS/FUS plays a role in spliceosome assembly.
Elsevier