High impact information on CTL1

• Mutagenesis of Ctl1p and Ace2p were unable to identify specific NES residues [1].
• These proteins are the 5' RNA triphosphatase Ctl1p, the cell cycle-regulated transcription factor Ace2p, and a protein encoded by the previously uncharacterized open reading frame YDR499W [1].
• CTL1 is not essential for cell viability and no genetic or physical interactions with the capping enzyme genes were observed [2].
• Recombinant Ctl1 protein releases gamma-phosphate from the 5'-end of RNA to produce a diphosphate terminus [2].
• Expression of CTL1 in myelinating structures of Torpedo marmorata [3].

Biological context of CTL1

• Selection and characterization of the choline transport mutation suppressor from Torpedo electric lobe, CTL1 [4].

Anatomical context of CTL1

• CTL1 immunolabeling was particularly conspicuous in the myelin sheath surrounding the electric nerve and in central myelinated structures [3].
• When full length torpedo CTL1 was expressed in oocytes, a broad 60 kDa band appeared concomitant with the detection of immunoreactivity at the plasma membrane [3].
• Northern analysis of Torpedo mRNA indicates that CTL1 is expressed at high levels in the spinal cord and brain [4].

Associations of CTL1 with chemical compounds

• The association of the presumptive choline transporter, CTL1, with myelin membranes suggests a role for this new protein in lipid production [3].

Other interactions of CTL1

• We initially isolated CTL1 from the electric lobe of brain through functional complementation of a yeast mutant deficient in choline transport [3].

References