作者: Stephen P Edmondson , John W Shriver
DOI: 10.1016/S0076-6879(01)34463-4
关键词: Peptide sequence 、 Sulfolobus solfataricus 、 DNA 、 Biochemistry 、 Recombinant DNA 、 Chromatin 、 RNase P 、 Sulfolobus acidocaldarius 、 Sulfolobus 、 Biology
摘要: Publisher Summary The chromatin of the archaea Sulfolobus acidocaldarius and solfataricus contains a number small basic proteins ranging in molecular weight from 7000 to 10,000. 7-kDa have been most studied believed be important DNA compaction stabilization duplex at growth temperatures 75° for S. 80° solfataricus. consist five species, designated Sac7a, b, c, d, e order increasing basicity. Sac7d (molecular 7477) Sac7e 7338) differ by six amino acid residues are coded distinct genes. Sac7a b carboxy-terminal truncated forms Sac7d. Only one form Sso7 has characterized; it is referred as Sso7d (MW 7019) based on homology structures both DNA-protein complexes also determined X-ray Crystallography. This chapter describes purification native Sac7 recombinant E. coli, along with brief description various physical properties purified proteins. Assays binding RNase activities described evaluated.