The description of the protein encoded in this ORF: heat shock protein 101
The translational frameshift (ribosome slippage) involved: 0
The ribosome read-through involved: no
The alternative forms of this protein occur by the alternative initiation of translation: no
The ORF absolute position (the base range includes START and STOP codons or their equivalents): 145-2883
Remarks:
The underlying mRNA sequence used for this record has start codon at base 145 instead of 147. It also lacks
the region of 60nt upstream the transcription start which has been included in the bicistronic tests. See
GI:68160574 for sequence of the relevant Zea mays chromosome region. Also, a full-length cDNA under
GI:223975968 has only 68bp as the 5'-UTR. A third mRNA sequence available has 114bp as the 5'-UTR
(GI:40060484).
Please refer also to sequence 39 from Patent WO03020928.
The IRES absolute position (the range includes START and STOP codons or their equivalents): 1-161
Conclusion: putative_IRES
How IRES boundaries were determined: guessed
The sequence of IRES region aligned to its secondary structure (if available):
Remarks:
In described experiment is Hsp101 5' UTR cloned in bicistronic plasmids contained chloramphenicol acetyl
transferase as first cistron and firefly luciferase as second cistron. The maize "Hsp101 5' UTR" used in the
bicistronic constructs included 60 nt upstream of the transcription start site, the entire 5' UTR (146 bp),
and the first 15 bp of the coding region in frame with the LUC ORF. Here is shown mRNA (UTR (146 nt) and open
reading frame (15 nt)) only. Therefore, T3/T7 capped transcripts used for in vitro translations contained in
roughly the first 60nt of a plant promoter. In vitro translation was let to proceed for 1 hour at 30
oC. FMDV Lb protease was supplemented to rabbit reticulocyte lysates used for translation of the bicistronic
mRNAs. Protein products were detected by antibodies. Alternatively, wheat germ extracts (and also rabbit
reticulocyte lysates) were depleted of eIF4E because plant eIF4G proteins are not susceptible to FMDV Lb
protease.