scholarly journals Mutational analysis of the 3' open reading frames and the splice junction at nucleotide 3225 of bovine papillomavirus type 1.

1987 ◽  
Vol 61 (12) ◽  
pp. 3889-3895 ◽  
Author(s):  
P L Hermonat ◽  
P M Howley
2010 ◽  
Vol 84 (10) ◽  
pp. 5448-5453 ◽  
Author(s):  
Mark D. Bennett ◽  
Andrea Reiss ◽  
Hans Stevens ◽  
Elisabeth Heylen ◽  
Marc Van Ranst ◽  
...  

ABSTRACT The first fully sequenced papillomavirus (PV) of marsupials, tentatively named Bettongia penicillata papillomavirus type 1 (BpPV1), was detected in papillomas from a woylie (Bettongia penicillata ogilbyi). The circular, double-stranded DNA genome contains 7,737 bp and encodes 7 open reading frames (ORFs), E6, E7, E1, E2, E4, L2, and L1, in typical PV conformation. BpPV1 is a close-to-root PV with L1 and L2 ORFs most similar to European hedgehog PV and bandicoot papillomatosis carcinomatosis virus types 1 and 2 (BPCV1 and -2). It appears that the BPCVs arose by recombination between an ancient PV and an ancient polyomavirus more than 10 million years ago.


2004 ◽  
Vol 78 (4) ◽  
pp. 2100-2113 ◽  
Author(s):  
Aare Abroi ◽  
Ivar Ilves ◽  
Sirje Kivi ◽  
Mart Ustav

ABSTRACT Recent studies have suggested that the tethering of viral genomes to host cell chromosomes could provide one of the ways to achieve their nuclear retention and partitioning during extrachromosomal maintenance in dividing cells. The data we present here provide firm evidence that the partitioning of the bovine papillomavirus type 1 (BPV1) genome is dependent on the chromatin attachment process mediated by viral E2 protein and its multiple binding sites. On the other hand, the attachment of E2 and the E2-mediated tethering of reporter plasmids to host chromosomes are not necessarily sufficient for efficient partitioning, suggesting that additional E2-dependent activities might be involved in the latter process. The activity of E2 protein in chromatin attachment and partitioning is more sensitive to the point mutations in the N-terminal domain than its transactivation and replication initiation functions. Therefore, at least part of the interactions of the E2 N-terminal domain with its targets during the chromatin attachment and partitioning processes are likely to involve specific receptors not involved in transactivation and replication activities of the protein. The mutational analysis also indicates that the binding of E2 to chromatin is not achieved through interaction of linear N-terminal subsequences of the E2 protein with putative receptors. Instead, the composite surface elements of the N-terminal domain build up the receptor-binding surface of E2. In this regard, the interaction of BPV1 E2 with its chromosomal targets clearly differs from the interactions of LANA1 protein from Kaposi's sarcoma-associated human herpesvirus and EBNA1 from Epstein-Barr virus with their specific receptors.


Genetics ◽  
1989 ◽  
Vol 121 (2) ◽  
pp. 393-393
Author(s):  
M Jakowec ◽  
P Prentki ◽  
M Chandler ◽  
D J Galas

Blood ◽  
1998 ◽  
Vol 92 (11) ◽  
pp. 4023-4030 ◽  
Author(s):  
Nico Ghilardi ◽  
Adrian Wiestner ◽  
Radek C. Skoda

Abstract Thrombopoietin (TPO) is a lineage-dominant hematopoietic cytokine that regulates megakaryopoiesis and platelet production. The major site of TPO biosynthesis is the liver. Despite easily detectable levels of liver TPO mRNA, the circulating TPO serum levels are very low. We have observed that translation of TPO mRNA is inhibited by the presence of inhibitory elements in the 5′-untranslated region (5′-UTR). Alternative promoter usage and differential splicing generate at least three TPO mRNA isoforms that differ in the composition of their 5′-UTR. Using mutational analysis we show that physiologically the translation of these TPO mRNA isoforms is strongly inhibited by the presence of AUG codons, which define several short open reading frames (ORFs) in the 5′-UTR and suppress efficient initiation at the physiologic start site. The two regularly spliced isoforms, which account for 98% of TPO mRNA, were almost completely inhibited, whereas a rare splice variant that lacks exon 2 can be more efficiently translated. Thus, inhibition of translation of the TPO mRNA is an efficient mechanism to prevent overproduction of this highly potent cytokine.


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