HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Choli, T. Articles by Reinhardt, R. Search for Related Content PubMed PubMed Citation Articles by Choli, T. Articles by Reinhardt, R. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 263, Issue 15, 7087-7093, May, 1988

Microsequence analysis of DNA-binding proteins 7a, 7b, and 7e from the archaebacterium Sulfolobus acidocaldarius

T Choli, B Wittmann-Liebold and R Reinhardt
Max-Planck-Institut fur Molekulare Genetik, Abteilung Wittmann, Berlin, Dahlem, West Germany.

DNA-binding proteins in eubacteria, such as Escherichia coli NS1 and NS2, are generally small basic molecules. In contrast, the archaebacterium Sulfolobus acidocaldarius contains three groups of DNA- binding proteins which have molecular masses of 7, 8, and 10 kDa. In the first group, five proteins (7a-7e) have been identified, while in the second and third group only two proteins each are present, denoted 8a and 8b and 10a and 10b, respectively. In this paper, we present the primary structures of proteins 7a, 7b, and 7e from the first group. All three proteins contain lysyl residues which are monomethylated to different extents. The modified lysines are found in the NH2-terminal regions of all 7-kDa proteins and in the COOH-terminal part of protein 7e. The sequences of the 7-kDa group are highly similar to each other. All of these macromolecules have been shown to interact specifically with DNA. Protein 7e of the 7-kDa group shows the tightest binding to DNA.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				J. Eichler and M. W. W. Adams Posttranslational Protein Modification in Archaea Microbiol. Mol. Biol. Rev., September 1, 2005; 69(3): 393 - 425. [Abstract] [Full Text] [PDF]

				H. Lou, Z. Duan, X. Huo, and L. Huang Modulation of Hyperthermophilic DNA Polymerase Activity by Archaeal Chromatin Proteins J. Biol. Chem., January 2, 2004; 279(1): 127 - 132. [Abstract] [Full Text] [PDF]

				H. Xue, R. Guo, Y. Wen, D. Liu, and L. Huang An Abundant DNA Binding Protein from the Hyperthermophilic Archaeon Sulfolobus shibatae Affects DNA Supercoiling in a Temperature-Dependent Fashion J. Bacteriol., July 15, 2000; 182(14): 3929 - 3933. [Abstract] [Full Text]

				V. Q. Mai, X. Chen, R. Hong, and L. Huang Small Abundant DNA Binding Proteins from the Thermoacidophilic Archaeon Sulfolobus shibatae Constrain Negative DNA Supercoils J. Bacteriol., May 1, 1998; 180(9): 2560 - 2563. [Abstract] [Full Text]

				A. Napoli, M. Kvaratskelia, M. F. White, M. Rossi, and M. Ciaramella A Novel Member of the Bacterial-Archaeal Regulator Family Is a Nonspecific DNA-binding Protein and Induces Positive Supercoiling J. Biol. Chem., March 30, 2001; 276(14): 10745 - 10752. [Abstract] [Full Text] [PDF]