Phosphorylation of human hnRNP protein A1 abrogates in vitro strand annealing activity (original) (raw)
Journal Article
,
Search for other works by this author on:
,
Search for other works by this author on:
,
1
Dipartimento di Biochimica, Universitá di Pavia
Via Tararnelli 3lb 27100 Pavia, Italy
Search for other works by this author on:
,
Search for other works by this author on:
Search for other works by this author on:
Received:
26 October 1992
Revision received:
19 January 1993
Accepted:
19 January 1993
Published:
25 February 1993
PDF Cite
Fabio Cobianchi, Cinzia Calvio, Monica Stoppini, Massimo Buvoli, Silvano Riva, Phosphorylation of human hnRNP protein A1 abrogates in vitro strand annealing activity, Nucleic Acids Research, Volume 21, Issue 4, 25 February 1993, Pages 949–955, https://doi.org/10.1093/nar/21.4.949
Close
Navbar Search Filter Mobile Enter search term Search
Abstract
In HeLa cells metabolically labeled in vlvo wlth [32P] orthophosphate in the presence of okadalc acid the concentration of phosphorylated A1 proteln was Increased slgnlflcantty as compared to controls. Purifled recombinant hnRNP protein A1 served as an excellent substrate in vitro for the catalytic subunit of cAMP-dependent proteln kinase (PKA) and for casein kinase II (CKII). Thin layer electrophoresls of A1 acld hydrolysates showed the proteln to be phosphorylated exclusively on serine residue by both kinases. V8 phosphopeptlde maps revealed that the target slte(s) of in vitro phosphorylatlon are located in the C-terminal reglon of A1. Phosphoamino acld sequence analysls and site dlrected mutagenesis identified Ser 199 as the sole phosphoamino acid in the protein phosphorylated by PKA. Phosphorylation Introduced by PKA resulted in the suppression qf the ablllty of proteln A1 to promote strand annealing in vitro, wlthout any detectable effect on Its nuclelc acld binding capacity. This flndlng indicates that phosphorylation of a single serlne resldue In the C-terminal domain may significantty alter the properties of protein A1.
This content is only available as a PDF.
© 1993 Oxford University Press
I agree to the terms and conditions. You must accept the terms and conditions.
Submit a comment
Name
Affiliations
Comment title
Comment
You have entered an invalid code
Thank you for submitting a comment on this article. Your comment will be reviewed and published at the journal's discretion. Please check for further notifications by email.
Citations
Views
Altmetric
Metrics
Total Views 57
15 Pageviews
42 PDF Downloads
Since 2/1/2017
| Month: | Total Views: |
|---|---|
| February 2017 | 5 |
| October 2017 | 1 |
| December 2017 | 4 |
| January 2018 | 6 |
| February 2018 | 5 |
| March 2018 | 4 |
| April 2018 | 3 |
| July 2018 | 1 |
| June 2019 | 1 |
| July 2019 | 1 |
| September 2020 | 1 |
| January 2021 | 1 |
| February 2021 | 1 |
| June 2022 | 1 |
| July 2022 | 1 |
| August 2022 | 2 |
| June 2023 | 2 |
| July 2023 | 1 |
| November 2023 | 1 |
| December 2023 | 1 |
| April 2024 | 2 |
| May 2024 | 3 |
| June 2024 | 3 |
| July 2024 | 1 |
| August 2024 | 2 |
| September 2024 | 2 |
| October 2024 | 1 |
Citations
90 Web of Science
×
Email alerts
Citing articles via
More from Oxford Academic