In this work we demonstrated that the inhibition of retrotransposition does not correlate with the binding of A3 proteins to the L1 retrotransposon ORF1p and that those proteins do not colocalise in the cells. Results of our study suggest that the inhibition occurs wither through interaction with ORF2p or through indirect interactions.
COBISS.SI-ID: 23252263
Transactivation response DNAbinding protein (TDP43) accumulation is the major component of protein inclusions found in patients with amyotrophic lateral sclerosis. TDP43 is predominantly located in the nucleus, however, in disease it mislocalizes to the cytoplasm where it aggregates to form inclusions. Knockdowns of karyopherinbeta and cellular apoptosis susceptibility protein resulted in marked cytoplasmic accumulation of TDP43. We propose that the latter protein associated with defective nuclear transport may play a mechanistic role in the pathogenesis of the TDP43 lobar degeneration.
COBISS.SI-ID: 23645223
Human APOBEC3G (hA3G), a member of the AID/APOBEC family of deaminases, is a restriction factor for human immunodeficiency virus (HIV). The role of mA3 in restriction of retroviral infection could be studied in mA3 -/- knockout mice, where the gene is inactivated. M-MuLV-infected mA3 -/- mice showed higher levels of infection at very early times compared to wild-type. M-MuLV-infected mA3 +/+ mice developed leukemia more slowly compared to animals lacking one or both copies of mA3 although the resulting disease was similar (T-lymphoma). These studies indicate that mA3 restricts M-MuLV in vivo.
COBISS.SI-ID: 22616871
TDP-43 is a predominantly nuclear protein that binds RNA and forms inclusion bodies in frontotemporal lobar degeneration (FTLD) and amyotrophic lateral sclerosis (ALS). We have found that TDP-43 preferentially binds long clusters of UG-rich sequences in vivo. Analysis of RNA binding by TDP-43 in FTLD brains revealed that the greatest increases in binding were to the MALAT1 and NEAT1 noncoding RNAs. Binding of TDP-43 to pre-mRNAs influenced alternative splicing in a similar position-dependent manner to Nova proteins. Many alternative mRNA isoforms regulated by TDP-43 encode proteins that regulate neuronal development or have been implicated in neurological diseases, highlighting the importance of TDP-43 for the regulation of splicing in the brain.
COBISS.SI-ID: 8278100