scholarly journals Two distinct regions of the murine p53 primary amino acid sequence are implicated in stable complex formation with simian virus 40 T antigen.

1988 ◽  
Vol 62 (10) ◽  
pp. 3903-3906 ◽  
Author(s):  
J R Jenkins ◽  
P Chumakov ◽  
C Addison ◽  
H W Stürzbecher ◽  
A Wade-Evans
Keyword(s):  
Amino Acid ◽  
Complex Formation ◽  
Amino Acid Sequence ◽  
Simian Virus 40 ◽  
Simian Virus ◽  
T Antigen ◽  
Stable Complex ◽  
Primary Amino Acid Sequence ◽  
Primary Amino

scholarly journals Hyperphosphorylation of the retinoblastoma gene product is determined by domains outside the simian virus 40 large-T-antigen-binding regions.

1990 ◽  
Vol 10 (12) ◽  
pp. 6586-6595 ◽  
Author(s):  
P A Hamel ◽  
B L Cohen ◽  
L M Sorce ◽  
B L Gallie ◽  
R A Phillips
Keyword(s):  
Cell Cycle ◽  
Complex Formation ◽  
Simian Virus 40 ◽  
Simian Virus ◽  
T Antigen ◽  
Phosphorylation Sites ◽  
Dependent Manner ◽  
Large T Antigen ◽  
T Complex ◽  
Cycle Dependent

With the murine retinoblastoma (RB) cDNA, a series of RB mutants were expressed in COS-1 cells and the pRB products were assessed for their ability (i) to bind to large T antigen (large T), (ii) to become modified by phosphorylation, and (iii) to localize in the nucleus. All point mutations and deletions introduced into regions previously defined as contributing to binding to large T abolished pRB-large T complex formation and prevented hyperphosphorylation of the RB protein. In contrast, a series of deletions 5' to these sites did not interfere with binding to large T. While some of the 5' deletion mutants were clearly phosphorylated in a cell cycle-dependent manner, one, delta Pvu, failed to be phosphorylated depsite binding to large T. pRB with mutations created at three putative p34cdc2 phosphorylation sites in the N-terminal region behaved similarly to wild-type pRB, whereas the construct delta P5-6-7-8, mutated at four serine residues C terminal to the large T-binding site, failed to become hyperphosphorylated despite retaining the ability to bind large T. All of the mutants described were also found to localize in the nucleus. These results demonstrate that the domains in pRB responsible for binding to large T are distinct from those recognized by the relevant pRB-specific kinase(s) and/or those which contain cell cycle-dependent phosphorylation sites. Furthermore, these data are consistent with a model in which cell cycle-dependent phosphorylation of pRB requires complex formation with other cellular proteins.

scholarly journals Intracellular Retention of the Corticotrophin-releasing Hormone (CRH) Precursor Within COS-7 Cells

1998 ◽  
Vol 46 (10) ◽  
pp. 1193-1197 ◽  
Author(s):  
Marcelo J. Perone ◽  
Simon Windeatt ◽  
Ewan Morrison ◽  
Andy Shering ◽  
Peter Tomasec ◽  
...  
Keyword(s):  
Amino Acid ◽  
Golgi Apparatus ◽  
Amino Acid Sequence ◽  
Protein Secretion ◽  
Intracellular Trafficking ◽  
Secretory Pathway ◽  
Intracellular Localization ◽  
Primary Amino Acid Sequence ◽  
Releasing Hormone ◽  
Primary Amino

We investigated the intracellular localization of CRH in transiently transfected COS-7 cells expressing the full-length rat corticotropin-releasing hormone (CRH) precursor cDNA. CRH synthesized by transfected COS-7 cells is mainly stored intracellularly. In contrast, CHO-K1 cells expressing the same CRH precursor stored and released equal amounts of immunoreactive (IR)-CRH. Ultrastructural analysis revealed that CRH is stored in electron-dense aggregates in the RER of transiently transfected COS-7 cells and does not migrate into the Golgi apparatus. On the basis of the different intracellular localization, storage, and release of CRH in COS-7 and CHO-K1 cells, we hypothesize that the intracellular trafficking of CRH within the constitutive secretory pathway for protein secretion not only depends on its primary amino acid sequence but might also be influenced by intracellular conditions or factors.

scholarly journals Amino acid sequence and the cellular location of the Na+-dependent d-glucose symporters (SGLT1) in the ovine enterocyte and the parotid acinar cell

1995 ◽  
Vol 312 (1) ◽  
pp. 293-300 ◽  
Author(s):  
P S Tarpey ◽  
I S Wood ◽  
S P Shirazi-Beechey ◽  
R B Beechey
Keyword(s):  
Plasma Membrane ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Acinar Cell ◽  
Acinar Cells ◽  
Amino Acid Sequences ◽  
Primary Amino Acid Sequence ◽  
Parotid Acinar Cells ◽  
Parotid Acinar Cell ◽  
Primary Amino

The Na(+)-dependent D-glucose symporter has been shown to be located on the basolateral domain of the plasma membrane of ovine parotid acinar cells. This is in contrast to the apical location of this transporter in the ovine enterocyte. The amino acid sequences of these two proteins have been determined. They are identical. The results indicated that the signals responsible for the differential targeting of these two proteins to the apical and the basal domains of the plasma membrane are not contained within the primary amino acid sequence.

CD156 (Human ADAM8): Expression, Primary Amino Acid Sequence, and Gene Location

Genomics ◽  
1997 ◽  
Vol 41 (1) ◽  
pp. 56-62 ◽  
Author(s):  
Kazuhiro Yoshiyama ◽  
Yasunori Higuchi ◽  
Masashi Kataoka ◽  
Keiko Matsuura ◽  
Shunsuke Yamamoto
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Gene Location ◽  
Primary Amino Acid Sequence ◽  
Primary Amino

scholarly journals DNA-binding properties of simian virus 40 T-antigen mutants defective in viral DNA replication.

1983 ◽  
Vol 3 (11) ◽  
pp. 1958-1966 ◽  
Author(s):  
C Prives ◽  
L Covey ◽  
A Scheller ◽  
Y Gluzman
Keyword(s):  
Amino Acid ◽  
Dna Sequences ◽  
Simian Virus 40 ◽  
Amino Acid Position ◽  
Simian Virus ◽  
T Antigen ◽  
Regulatory Sequences ◽  
Viral Dna ◽  
Viral Origin ◽  
Specific Affinity

Three simian virus 40 (SV40)-transformed monkey cell lines, C2, C6, and C11, producing T-antigen variants that are unable to initiate viral DNA replication, were analyzed with respect to their affinity for regulatory sequences at the viral origin of replication. C2 and C11 T antigens both bound specifically to sequences at sites 1 and 2 at the viral origin region, whereas C6 T antigen showed no specific affinity for any viral DNA sequences under all conditions tested. Viral DNA sequences encoding the C6 T antigen have recently been cloned out of C6 cells and used to transform an established rat cell line. T antigen from several cloned C6-SV40-transformed rat lines failed to bind specifically to the origin. C6 DNA contains three mutations: two located close to the amino terminus of T antigen at amino acid positions 30 and 51 and a third located internally at amino acid position 153. Two recombinant SV40 DNA mutants were prepared containing either the amino-terminal mutations at positions 30 and 51 (C6-1) or the internally located mutation at position 153 (C6-2) and used to transform Rat 2 cells. Whereas T antigen from C6-2-transformed cells lacked any specific affinity for these sequences. Therefore, the single mutation at amino acid position 153 (Asn leads to Thr) is sufficient to abolish the origin-binding property of T antigen. A T antigen-specific monoclonal antibody, PAb 100, which had been previously shown to immunoprecipitate an immunologically distinct origin-binding subclass of T antigen, recognized wild-type or C6-1 antigens, but failed to react with C6 or C6-2 T antigens. These results indicate that viral replication function comprises properties of T antigen that exist in addition to its ability to bind specifically to the SV40 regulatory sequences. Furthermore, it is concluded from these data that specific viral origin binding is not a necessary feature of the transforming function of T antigen.

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