Prediction of an HMG-box fold in the C-terminal domain of histone H1: Insights into its role in DNA condensation

被引:31
作者
Bharath, MMS
Chandra, NR
Rao, MRS [1 ]
机构
[1] Indian Inst Sci, Dept Biochem, Bangalore 560012, Karnataka, India
[2] Indian Inst Sci, Bioinformat Ctr, Bangalore 560012, Karnataka, India
关键词
HMG-box fold; histone H1; DNA condensation; C-terminal domain; chromatin organization;
D O I
10.1002/prot.10204
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
In eukaryotes, histone H1 promotes the organization of polynucleosome filaments into chromatin fibers, thus contributing to the formation of an important structural framework responsible for various DNA transaction processes. The H1 protein consists of a short N-terminal "nose," a central globular domain, and a highly basic C-terminal domain. Structure prediction of the C-terminal domain using fold recognition methods reveals the presence of an HMG-box-like fold. We recently showed by extensive site-directed and deletion mutagenesis studies that a 34 amino acid segment encompassing the three S/TPKK motifs, within the C-terminal domain, is responsible for DNA condensing properties of H1. The position of these motifs in the predicted structure corresponds exactly to the DNA-binding segments of HMG-box-containing proteins such as Lef-1 and SRY. Previous analyses have suggested that histone H1 is likely to bend DNA bound to the C-terminal domain, directing the path of linker DNA in chromatin. Prediction of the structure of this domain provides a framework for understanding the higher order of chromatin organization. (C) 2002 Wiley-Liss, Inc.
引用
收藏
页码:71 / 81
页数:11
相关论文
共 56 条
  • [1] REGULATION OF THE HIGHER-ORDER STRUCTURE OF CHROMATIN BY HISTONES-H1 AND HISTONES-H5
    ALLAN, J
    COWLING, GJ
    HARBORNE, N
    CATTINI, P
    CRAIGIE, R
    GOULD, H
    [J]. JOURNAL OF CELL BIOLOGY, 1981, 90 (02) : 279 - 288
  • [2] Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
    Altschul, SF
    Madden, TL
    Schaffer, AA
    Zhang, JH
    Zhang, Z
    Miller, W
    Lipman, DJ
    [J]. NUCLEIC ACIDS RESEARCH, 1997, 25 (17) : 3389 - 3402
  • [3] The InterPro database, an integrated documentation resource for protein families, domains and functional sites
    Apweiler, R
    Attwood, TK
    Bairoch, A
    Bateman, A
    Birney, E
    Biswas, M
    Bucher, P
    Cerutti, T
    Corpet, F
    Croning, MDR
    Durbin, R
    Falquet, L
    Fleischmann, W
    Gouzy, J
    Hermjakob, H
    Hulo, N
    Jonassen, I
    Kahn, D
    Kanapin, A
    Karavidopoulou, Y
    Lopez, R
    Marx, B
    Mulder, NJ
    Oinn, TM
    Pagni, M
    Servant, F
    Sigrist, CJA
    Zdobnov, EM
    [J]. NUCLEIC ACIDS RESEARCH, 2001, 29 (01) : 37 - 40
  • [4] PRINTS - A PROTEIN MOTIF FINGERPRINT DATABASE
    ATTWOOD, TK
    BECK, ME
    [J]. PROTEIN ENGINEERING, 1994, 7 (07): : 841 - 848
  • [5] Protein structure prediction and structural genomics
    Baker, D
    Sali, A
    [J]. SCIENCE, 2001, 294 (5540) : 93 - 96
  • [6] Pfam 3.1: 1313 multiple alignments and profile HMMs match the majority of proteins
    Bateman, A
    Birney, E
    Durbin, R
    Eddy, SR
    Finn, RD
    Sonnhammer, ELL
    [J]. NUCLEIC ACIDS RESEARCH, 1999, 27 (01) : 260 - 262
  • [7] Identification of a 34 amino acid stretch within the C-terminus of histone H1 as the DNA-condensing domain by site-directed mutagenesis
    Bharath, MMS
    Ramesh, S
    Chandra, NR
    Rao, MRS
    [J]. BIOCHEMISTRY, 2002, 41 (24) : 7617 - 7627
  • [8] Bustin M, 1996, PROG NUCLEIC ACID RE, V54, P35, DOI 10.1016/S0079-6603(08)60360-8
  • [9] Dinucleosomes show compaction by ionic strength, consistent with bending of linker DNA
    Butler, PJG
    Thomas, JO
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 1998, 281 (03) : 401 - 407
  • [10] HOMONUCLEAR AND HETERONUCLEAR 2-DIMENSIONAL NMR-STUDIES OF THE GLOBULAR DOMAIN OF HISTONE-H1 - SEQUENTIAL ASSIGNMENT AND SECONDARY STRUCTURE
    CERF, C
    LIPPENS, G
    MUYLDERMANS, S
    SEGERS, A
    RAMAKRISHNAN, V
    WODAK, SJ
    HALLENGA, K
    WYNS, L
    [J]. BIOCHEMISTRY, 1993, 32 (42) : 11345 - 11351