The novel SAR-binding domain of scaffold attachment factor A (SAF-A) is a target in apoptotic nuclear breakdown

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1997
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Göhring, Frank
Schwab, Birgit L.
Fackelmayer, Frank O.
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The EMBO Journal. 1997, 16(24), pp. 7361-7371. ISSN 0261-4189. eISSN 1460-2075. Available under: doi: 10.1093/emboj/16.24.7361
Zusammenfassung

The scaffold attachment factor A (SAF-A) is an abundant component of the nuclear scaffold and of chromatin, and also occurs in heterogeneous nuclear ribonucleoprotein (hnRNP) complexes. Evidence from previous experiments had suggested that SAF-A most likely has at least two different functions, being involved both in nuclear architecture and RNA metabolism. We now show that the protein has a novel scaffold-associated region (SAR)-specifi bipartite DNA-binding domain which is independent from the previously identifie RNA-binding domain, the RGG box. During apoptosis, but not during necrosis, SAF-A is cleaved in a caspasedependent way. Cleavage occurs within the bipartite DNA-binding domain, resulting in a loss of DNAbinding activity and a concomitant detachment of SAF-A from nuclear structural sites. On the other hand, cleavage does not compromise the association of SAF-A with hnRNP complexes, indicating that the function of SAF-A in RNA metabolism is not affected in apoptosis. Our results suggest that detachment of SAF-A from SARs, caused by apoptotic proteolysis of its DNA-binding domain, is linked to the formation of oligonucleosomal-sized DNA fragments and could therefore contribute to nuclear breakdown in apoptotic cells.

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570 Biowissenschaften, Biologie
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ISO 690GÖHRING, Frank, Birgit L. SCHWAB, Pierluigi NICOTERA, Marcel LEIST, Frank O. FACKELMAYER, 1997. The novel SAR-binding domain of scaffold attachment factor A (SAF-A) is a target in apoptotic nuclear breakdown. In: The EMBO Journal. 1997, 16(24), pp. 7361-7371. ISSN 0261-4189. eISSN 1460-2075. Available under: doi: 10.1093/emboj/16.24.7361
BibTex
@article{Gohring1997novel-8454,
  year={1997},
  doi={10.1093/emboj/16.24.7361},
  title={The novel SAR-binding domain of scaffold attachment factor A (SAF-A) is a target in apoptotic nuclear breakdown},
  number={24},
  volume={16},
  issn={0261-4189},
  journal={The EMBO Journal},
  pages={7361--7371},
  author={Göhring, Frank and Schwab, Birgit L. and Nicotera, Pierluigi and Leist, Marcel and Fackelmayer, Frank O.}
}
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    <dcterms:abstract xml:lang="eng">The scaffold attachment factor A (SAF-A) is an abundant component of the nuclear scaffold and of chromatin, and also occurs in heterogeneous nuclear ribonucleoprotein (hnRNP) complexes. Evidence from previous experiments had suggested that SAF-A most likely has at least two different functions, being involved both in nuclear architecture and RNA metabolism. We now show that the protein has a novel scaffold-associated region (SAR)-specifi bipartite DNA-binding domain which is independent from the previously identifie RNA-binding domain, the RGG box. During apoptosis, but not during necrosis, SAF-A is cleaved in a caspasedependent way. Cleavage occurs within the bipartite DNA-binding domain, resulting in a loss of DNAbinding activity and a concomitant detachment of SAF-A from nuclear structural sites. On the other hand, cleavage does not compromise the association of SAF-A with hnRNP complexes, indicating that the function of SAF-A in RNA metabolism is not affected in apoptosis. Our results suggest that detachment of SAF-A from SARs, caused by apoptotic proteolysis of its DNA-binding domain, is linked to the formation of oligonucleosomal-sized DNA fragments and could therefore contribute to nuclear breakdown in apoptotic cells.</dcterms:abstract>
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