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Proteins non-histone

SADP or sulfo-SADP also have been used to study the phenylalanine-methionine-arginine-phenylalanine-amide-activated sodium channel (Coscoy et al., 1998), various apolipoprotein E isoforms (Mann et al., 1995), the high-affinity phenylalkylamine Ca2+ antagonist binding protein from guinea pig (Moebius et al., 1994), the interaction of non-histone proteins with nucleosome core particles (Reeves and Nissen, 1993), and the interactions among cytochromes P-450 in the endoplasmic reticulum (Alston et al., 1991). See Chapter 28 for methods of using photoreactive heterobifunctional crosslinkers to study protein interactions. [Pg.316]

Another group of non-histone proteins have been identified as essential components for the formation of the condensed chromosome (Table 1). Topoisomerase II (topo II) localizes in the scaffold/matrix fraction of the interphase nuclear (Berrios et al., 1985) and the mitotic chromosome (Maeshima and Laemmli, 2003) (see section 3.1). Topo II forms a ring-shaped homodimer (Berger et al, 1996 Nettikadan et al, 1998) and catalyzes the decatenation and relaxation of DNA double strand (Wang, 2002). In fission yeast, chromosomes cannot be condensed without functional topo II (Uemura et al, 1987). In addition, in in vitro experiment, mitotic extracts containing topo II induce chromatin condensation in the isolated nuclei from HeLa and chicken erythrocyte cells (Adachi et al., 1991). [Pg.10]

DNA is packaged in the nucleus into the form of chromatin. Chromatin is a nucleoprotein complex composed of histone and non-histone proteins, DNA and RNA and it exhibits a repeating structure (van Holde, 1988). The basal unit of chromatin, the nucleosome, is composed of a histone octamer (two each of H2A, H2B, H3 and H4) around which two superhelical turns of DNA are wrapped (van Holde, 1988). The structure of both the histone octamer (Arents et al, 1991)... [Pg.71]

More recent studies in Drosophila revealed that H3.3 also plays an important role in the male pronucleus after fertilization (Loppin et al. 2005). The loss of the H3.3 chaperone HIRA impairs the replacement of paternal non-histone proteins from the sperm nucleus with maternally provided histones including H3.3, while the maternal genome exclusively contains the canonical H3. Thus, H3.3 and its deposition factor HIRA function in early fertilization events and might have a role in imprinting in higher eukaryotes. [Pg.95]

Olson MO, Ezrailson EG, Guetzow K, Busch H (1975) Localization and phosphorylation of nuclear, nucleolar and extranucleolar non-histone proteins of Novikoff hepatoma ascites cells. J Mol Biol 97 611-619... [Pg.142]

Figure 1. Mechanistic effect of acetylation/deacetylation of histones and nonhistones on chromatin stracture.(a) Acetylation of non-histone proteins results in transcriptional activation (b) Acetylation of ORCl by HBOl is important for replication, (c) Acetylation of newly synthesized... Figure 1. Mechanistic effect of acetylation/deacetylation of histones and nonhistones on chromatin stracture.(a) Acetylation of non-histone proteins results in transcriptional activation (b) Acetylation of ORCl by HBOl is important for replication, (c) Acetylation of newly synthesized...
ROLE OF NON HISTONE PROTEINS ACETYLATION ON CELLULAR FUNCTION... [Pg.195]

Table 1. Biochemical and cellular functions of non-histone protein acetylation pEnhances-... Table 1. Biochemical and cellular functions of non-histone protein acetylation pEnhances-...
Cell cycle progression, apoptosis, DNA damage and DNA repair are cellular functions that are regulated by several mechanisms. One such important regulatory mechanism is posttranslational modification of histone and non-histone proteins. Myriad of reports have been shown that acetylation of non-histone proteins apart from histones, contributes in major to these processes. [Pg.201]

Acetylation levels of histone and non-histone proteins are regulated upon DNA damage. Retinoblastoma protein pRb controls Gl-S phase transition and phosphorylation of pRb regulates it function. DNA damage induced acetylation of pRb near the phosphorylation sites prevents it phosphorylation and keep pRb in active form thereby leading to growth repression. DNA damage dependant association... [Pg.203]

Aberrant acetylation levels of non histone proteins not only lead to the dysfunction of these proteins but also cause disturbances in cellular processes thereby leading to several diseases (Fig. 3). There are several reports of aberrant acetylation in diseases like cancer, diabetes, cardiac hypertrophy and viral diseases. [Pg.204]

Glozak MA, Sengupta N, Zhang X, Seto E (2005) Acetylation and deacetylation of non-histone proteins. Gene 363 15-23... [Pg.366]

The spectrum of pleiotropic functions of different HI variants in different taxa has yet to be established. With respect to interactions within chromatin, the elucidation of the role of linker histones in transmitting or enhancing the effects of other non-histone proteins will be of particular interest. Given the dynamic behavior of HI in the nucleus, the possibility of auxiliary extrachromosomal functions performed by the free HI pool should be explored. An example of such a function is the recent finding that free HI is involved in the import of adenovirus DNA into the nucleus [158]. Other potential functions, especially at the period of maximum chromatin condensation, could depend on the gradient of free HI around the chromosomes. [Pg.98]

The first indication that modification of specific tail residues were linked to chromatin functional states, came from immunostaining of Drosophila polytene chromosomes with antibodies specific for H4 acetylated at defined lysines [13]. As shown in Fig. 2A, H4 acetylated at lysine 16 (H4acK16) was found almost exclusively on the transcriptional hyperactive male X chromosome (Fig. 2). (Genes on the Drosophila male X are transcribed twice as fast as their female counterparts so as to equalize levels of X-linked gene products between XY males and XX females.) In addition, H4 lysine 12 was found to remain acetylated in centric heterochromatin, while lysines 5, 8, and 16 were all under-acetylated [13]. These observations led to the suggestion that the histone N-terminal tails constitute nucleosome surface markers that can be recognized by non-histone proteins in a modification-dependent manner to alter the functional state of chromatin [13]. [Pg.293]

The nucleus is not capable of synthesizing proteins. All of the nuclear proteins therefore have to be imported—the histones with which DNA is associated in chromatin, and also the so-called non-histone proteins (DNA polymerases and RNA polymerases, auxiliary and structural proteins, transcription factors, and ribosomal proteins). Ribosomal RNA (rRNA) already associates with proteins in the nucleolus to form ribosome precursors. [Pg.208]

The non-histone proteins are very heterogeneous. This group includes structural proteins of the nucleus, as well as many enzymes and transcription factors (see p. 118), which selectively bind to specific segments of DNA and regulate gene expression and other processes. [Pg.238]


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See also in sourсe #XX -- [ Pg.135 ]

See also in sourсe #XX -- [ Pg.145 , Pg.169 ]




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Histone

Non-histone chromosomal protein

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