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A novel hnRNP protein (HAP/SAF-B) enters a subset of hnRNP complexes and relocates in nuclear granules in response to heat shock.
J Cell Sci. 1999 May; 112 (Pt 10):1465-76.JC

Abstract

A two-hybrid screening in yeast for proteins interacting with the human hnRNP A1, yielded a nuclear protein of 917 amino acids that we termed hnRNP A1 associated protein (HAP). HAP contains an RNA binding domain (RBD) flanked by a negatively charged domain and by an S/K-R/E-rich region. In in vitro pull-down assays, HAP interacts with hnRNP A1, through its S/K-R/E-rich region, and with several other hnRNPs. HAP was found to be identical to the previously described Scaffold Attachment Factor B (SAF-B) and to HET, a transcriptional regulator of the Heat Shock Protein 27 gene. We show that HAP is a bona fide hnRNP protein, since anti-HAP antibodies immunoprecipitate from HeLa cell nucleoplasm the complete set of hnRNP proteins. Unlike most hnRNP proteins, the subnuclear distribution of HAP is profoundly modified in heat-shocked HeLa cells. Heat-shock treatment at 42 degrees C causes a transcription-dependent recruitment of HAP to a few large nuclear granules that exactly coincide with sites of accumulation of Heat Shock Factor 1 (HSF1). The recruitment of HAP to the granules is temporally delayed with respect to HSF1 and persists for a longer time during recovery at 37 degrees C. The hnRNP complexes immunoprecipitated from nucleoplasm of heat-shocked cells with anti-HAP antibodies have an altered protein composition with respect to canonical complexes. Altogether our results suggest an involvement of HAP in the cellular response to heat shock, possibly at the RNA metabolism level.

Authors+Show Affiliations

Istituto di Genetica Biochimica ed Evoluzionistica, CNR Via Abbiategrasso 207, Italy.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

10212141

Citation

Weighardt, F, et al. "A Novel hnRNP Protein (HAP/SAF-B) Enters a Subset of hnRNP Complexes and Relocates in Nuclear Granules in Response to Heat Shock." Journal of Cell Science, vol. 112 (Pt 10), 1999, pp. 1465-76.
Weighardt F, Cobianchi F, Cartegni L, et al. A novel hnRNP protein (HAP/SAF-B) enters a subset of hnRNP complexes and relocates in nuclear granules in response to heat shock. J Cell Sci. 1999;112 (Pt 10):1465-76.
Weighardt, F., Cobianchi, F., Cartegni, L., Chiodi, I., Villa, A., Riva, S., & Biamonti, G. (1999). A novel hnRNP protein (HAP/SAF-B) enters a subset of hnRNP complexes and relocates in nuclear granules in response to heat shock. Journal of Cell Science, 112 (Pt 10), 1465-76.
Weighardt F, et al. A Novel hnRNP Protein (HAP/SAF-B) Enters a Subset of hnRNP Complexes and Relocates in Nuclear Granules in Response to Heat Shock. J Cell Sci. 1999;112 (Pt 10):1465-76. PubMed PMID: 10212141.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - A novel hnRNP protein (HAP/SAF-B) enters a subset of hnRNP complexes and relocates in nuclear granules in response to heat shock. AU - Weighardt,F, AU - Cobianchi,F, AU - Cartegni,L, AU - Chiodi,I, AU - Villa,A, AU - Riva,S, AU - Biamonti,G, PY - 1999/4/23/pubmed PY - 1999/4/23/medline PY - 1999/4/23/entrez SP - 1465 EP - 76 JF - Journal of cell science JO - J Cell Sci VL - 112 (Pt 10) N2 - A two-hybrid screening in yeast for proteins interacting with the human hnRNP A1, yielded a nuclear protein of 917 amino acids that we termed hnRNP A1 associated protein (HAP). HAP contains an RNA binding domain (RBD) flanked by a negatively charged domain and by an S/K-R/E-rich region. In in vitro pull-down assays, HAP interacts with hnRNP A1, through its S/K-R/E-rich region, and with several other hnRNPs. HAP was found to be identical to the previously described Scaffold Attachment Factor B (SAF-B) and to HET, a transcriptional regulator of the Heat Shock Protein 27 gene. We show that HAP is a bona fide hnRNP protein, since anti-HAP antibodies immunoprecipitate from HeLa cell nucleoplasm the complete set of hnRNP proteins. Unlike most hnRNP proteins, the subnuclear distribution of HAP is profoundly modified in heat-shocked HeLa cells. Heat-shock treatment at 42 degrees C causes a transcription-dependent recruitment of HAP to a few large nuclear granules that exactly coincide with sites of accumulation of Heat Shock Factor 1 (HSF1). The recruitment of HAP to the granules is temporally delayed with respect to HSF1 and persists for a longer time during recovery at 37 degrees C. The hnRNP complexes immunoprecipitated from nucleoplasm of heat-shocked cells with anti-HAP antibodies have an altered protein composition with respect to canonical complexes. Altogether our results suggest an involvement of HAP in the cellular response to heat shock, possibly at the RNA metabolism level. SN - 0021-9533 UR - https://www.unboundmedicine.com/medline/citation/10212141/A_novel_hnRNP_protein__HAP/SAF_B__enters_a_subset_of_hnRNP_complexes_and_relocates_in_nuclear_granules_in_response_to_heat_shock_ L2 - http://jcs.biologists.org/cgi/pmidlookup?view=long&pmid=10212141 DB - PRIME DP - Unbound Medicine ER -