Mammalian Hsp70 and Hsp110 proteins bind to RNA motifs involved in mRNA stability

Tamás Henics, Eszter Nagy, Hyun Ju Oh, P. Csermely, Alexander Von Gabain, John R. Subjeck

Research output: Contribution to journalArticle

94 Citations (Scopus)

Abstract

In this study, in vitro RNA binding by members of the mammalian 70-kDa heat shock protein (Hsp) family was examined. We show that Hsp/Hsc70 and Hsp110 proteins preferentially bound AU-rich RNA in vitro. Inhibition of RNA binding by ATP suggested the involvement of the N-terminal ATP-binding domain. By using deletion mutants of Hsp110 protein, a diverged Hsp70 family member, RNA binding was localized to the N-terminal ATP-binding domain of the molecule. The C-terminal peptide-binding domain did not bind RNA, but its engagement by a peptide substrate abrogated RNA binding by the N terminus of the protein. Interestingly, removal of the C-terminal α-helical structure or the α-loop domain unique to Hsp110 immediately downstream of the peptide- binding domain, but not both, resulted in considerably increased RNA binding as compared with the wild type protein. Finally, a 70-kDa activity was immunoprecipitated from RNA-protein complexes formed in vitro between cytoplasmic proteins of human lymphocytes and AU-rich RNA. These findings support the idea that certain heat shock proteins may act as RNA-binding entities in vivo to guide the appropriate folding of RNA substrates for subsequent regulatory processes such as mRNA degradation and/or translation.

Original languageEnglish
Pages (from-to)17318-17324
Number of pages7
JournalJournal of Biological Chemistry
Volume274
Issue number24
DOIs
Publication statusPublished - Jun 11 1999

Fingerprint

Nucleotide Motifs
RNA Stability
RNA
Messenger RNA
Proteins
Adenosine Triphosphate
HSP110 Heat-Shock Proteins
Heat-Shock Proteins
Peptides
HSC70 Heat-Shock Proteins
RNA Folding
HSP70 Heat-Shock Proteins
Protein Biosynthesis
Lymphocytes
Mutant Proteins
Substrates

ASJC Scopus subject areas

  • Biochemistry

Cite this

Mammalian Hsp70 and Hsp110 proteins bind to RNA motifs involved in mRNA stability. / Henics, Tamás; Nagy, Eszter; Oh, Hyun Ju; Csermely, P.; Von Gabain, Alexander; Subjeck, John R.

In: Journal of Biological Chemistry, Vol. 274, No. 24, 11.06.1999, p. 17318-17324.

Research output: Contribution to journalArticle

Henics, Tamás ; Nagy, Eszter ; Oh, Hyun Ju ; Csermely, P. ; Von Gabain, Alexander ; Subjeck, John R. / Mammalian Hsp70 and Hsp110 proteins bind to RNA motifs involved in mRNA stability. In: Journal of Biological Chemistry. 1999 ; Vol. 274, No. 24. pp. 17318-17324.
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