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Characterization of novel elongated Parvulin isoforms that are ubiquitously expressed in human tissues and originate from alternative transcription initiation
The existence of a longer Parvulin isoform expressed in all tissues examined so far is confirmed by RT-PCR and the N-terminal elongation of Par 17-QR and Par17-RS suggests these isoforms to perform divergent functions within the eukaryotic cell than the well characterized Par14. Expand
The DNA binding parvulin Par17 is targeted to the mitochondrial matrix by a recently evolved prepeptide uniquely present in Hominidae
The DNA binding parvulin Par17 is targeted to the mitochondrial matrix by the most recently evolved mitochondrial prepeptide known to date, thus adding a novel protein constituent to the mtDNA proteome of Hominidae. Expand
Human TPST1 transmembrane domain triggers enzyme dimerisation and localisation to the Golgi compartment.
In vivo FRET studies using the transmembrane domain suggest that the human tyrosylprotein sulfotransferase may be functional as homodimer/oligomer in the trans-Golgi compartment. Expand
Heterodimers of tyrosylprotein sulfotransferases suggest existence of a higher organization level of transferases in the membrane of the trans-Golgi apparatus.
The formation of TPST/TPST2 heterodimers and a novel interaction between either TPST1 or TPST2 and the α-2,6-sialyltransferase are reported, indicating a higher organization level of tyrosylprotein sulfotransferases that may serve for substrate selectivity and/or effective organization of multiple post-translational modification of proteins. Expand
Determinants of tyrosylprotein sulfation coding and substrate specificity of tyrosylprotein sulfotransferases in metazoans.
This short review likes to give a historical view on the discovery of metazoan Tyrosylprotein Sulfotransferases (TPSTs) setting its focus on the determinants of substrate specificity of these enzymesExpand