共查询到20条相似文献,搜索用时 31 毫秒
1.
2.
3.
4.
Leslie E Carlini Michael J Getz Arthur R Strauch Robert J Kelm 《The Journal of biological chemistry》2002,277(10):8682-8692
5.
6.
7.
Knapp AM Ramsey JE Wang SX Strauch AR Kelm RJ 《The Journal of biological chemistry》2007,282(49):35899-35909
8.
9.
Knapp AM Ramsey JE Wang SX Godburn KE Strauch AR Kelm RJ 《The Journal of biological chemistry》2006,281(12):7907-7918
10.
11.
12.
Shimotai Y Minami H Saitoh Y Onodera Y Mishima Y Kelm RJ Tsutsumi K 《Biochemical and biophysical research communications》2006,340(2):517-525
The rat aldolase B promoter acts as a replication origin in vivo, as well as an autonomously replicating sequence (ARS). Here, we examined roles of a polypurine stretch (site PPu) in this origin, which is indispensable to the ARS activity. Purification of site PPu-binding protein revealed that site PPu binds Puralpha and Purbeta, i.e., single-stranded DNA-binding proteins whose roles in replication have been implicated, but less clear. Biochemical analyses showed that site PPu even in a longer DNA fragment is unstable in terms of double-helix, implying that Puralpha/beta may stabilize single-stranded state. Deletion of site PPu from the origin DNA, which was ectopically positioned in the mouse chromosome, significantly reduced replicator activity. Chromatin immunoprecipitation experiments showed that deletion of site PPu abolishes binding of the Puralpha/beta proteins to the origin. These observations suggest functional roles of site PPu and Puralpha/beta proteins in replication initiation. 相似文献
13.
Induction of vascular smooth muscle alpha-actin gene transcription in transforming growth factor beta1-activated myofibroblasts mediated by dynamic interplay between the Pur repressor proteins and Sp1/Smad coactivators
下载免费PDF全文
![点击此处可从《Molecular biology of the cell》网站下载免费的PDF全文](/ch/ext_images/free.gif)
Subramanian SV Polikandriotis JA Kelm RJ David JJ Orosz CG Strauch AR 《Molecular biology of the cell》2004,15(10):4532-4543
14.
15.
16.
Delineation of the high-affinity single-stranded telomeric DNA-binding domain of Saccharomyces cerevisiae Cdc13
下载免费PDF全文
![点击此处可从《Nucleic acids research》网站下载免费的PDF全文](/ch/ext_images/free.gif)
Cdc13 is an essential protein from Saccharomyces cerevisiae that caps telomeres by protecting the C-rich telomeric DNA strand from degradation and facilitates telomeric DNA replication by telomerase. In vitro, Cdc13 binds TG-rich single-stranded telomeric DNA with high affinity and specificity. A previously identified domain of Cdc13 encompassing amino acids 451–694 (the 451–694 DBD) retains the single-stranded DNA-binding properties of the full-length protein; however, this domain contains a large unfolded region identified in heteronuclear NMR experiments. Trypsin digestion and MALDI mass spectrometry were used to identify the minimal DNA-binding domain (the 497–694 DBD) necessary and sufficient for full DNA-binding activity. This domain was completely folded, and the N-terminal unfolded region removed was shown to be dispensable for function. Using affinity photocrosslinking to site-specifically modified telomeric single-stranded DNA, the 497–694 DBD was shown to contact the entire 11mer required for high-affinity binding. Intriguingly, both domains bound single-stranded telomeric DNA with much greater affinity than the full-length protein. The full-length protein exhibited the same rate of dissociation as both domains, however, indicating that the full-length protein contains a region that inhibits association with single-stranded telomeric DNA. 相似文献
17.
18.
Atrial natriuretic peptide clearance receptor. Complete sequence and functional expression of cDNA clones 总被引:23,自引:0,他引:23
F Fuller J G Porter A E Arfsten J Miller J W Schilling R M Scarborough J A Lewicki D B Schenk 《The Journal of biological chemistry》1988,263(19):9395-9401
The major class of atrial natriuretic peptide (ANP) receptors was isolated from cultured vascular smooth muscle cells, and a partial amino acid sequence was obtained. This allowed the isolation of cDNA clones from which the entire amino acid sequence was established. The smooth muscle cell ANP receptor appears to be synthesized as a 537-amino acid precursor with an N-terminal membrane translocation signal. The mature form consists of 496 amino acids with a single potential transmembrane domain predicting a 37-amino acid cytoplasmic domain and a large, acidic, extracellular domain low in cysteine and probably containing attached carbohydrate. The receptor is therefore similar in structure to the growth factor receptors but notably lacks repetitive cysteine-rich domains and has a relatively small intracellular domain. Expression of the cloned receptor in Xenopus oocytes elicited high affinity, membrane-associated binding sites for ANP and for truncated and internally deleted analogs of ANP. These results reflect the ligand binding specificity found for the major class of ANP receptors on smooth muscle cells and thus provide additional evidence that two distinct ANP receptors exist since ANP receptor-coupled guanylate cyclase activity exhibits a very different ANP analog specificity. 相似文献
19.