Title : Physical and biochemical properties of mammalian
DNase X proteins : non-AUG translation initiation of porcine and bovine mRNAs for
DNase X .
DNase X is the first human
DNase protein identified as being homologous with
DNase I
Abstract :
- In the present study we describe the isolation of several mammalian DNase X cDNAs and the molecular characterization of their coding proteins
- A sequence comparison reveals some conserved characteristics: all the mammalian DNase X proteins have an N-terminal signal peptide , a potential N-linked glycosylation site and a C-terminal hydrophobic domain
- Human DNase X , ectopically expressed in HeLa S3 cells, is located in the ER (endoplasmic reticulum) and is modified by an N-linked glycosylation at Asn-243
- Gene expression analyses show that the high expression level in muscular tissues, a known feature of human DNASE X , is also observed in mouse DNase X . Interestingly, the translation of porcine and bovine DNase X proteins occurs in the absence of an in-frame AUG initiation codon
- We show that their mRNAs utilize a conserved CUG triplet for translation initiation
Output (sent_index, trigger,
protein,
sugar,
site):
- 2. glycosylation, , -, -, site
- 3. glycosylation, , -, -, Asn-243
Output(Part-Of) (sent_index,
protein,
site):
- 2. DNase X proteins, domain
- 2. DNase X proteins, peptide
- 2. DNase X proteins, site
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):
- 3. DNase X cDNAs, -, Asn-243