High mobility group like chromosomal proteins from amebas of the acellular slime mold Physarum polycephalum

Côté, Serge; Neelin, J. M.; Pallotta, Dominick

doi:10.1021/bi00328a035

Cited by 8 publications

(11 citation statements)

References 38 publications

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“…A comparison of the immunological relationship between plant and animal HMG proteins using a quantitative blotting procedure indicates only a very low degree of cross reactivity between the plant and animal proteins (Spiker and Everett 1987). Attempts at identifying HMG proteins in other taxa have led to similar equivocal results (Hamana and Iwai 1979, Weber and Isenberg 1980, Bassuk and Mayfield 1982, Marquez et al 1982, Mayes 1982, Levy et al 1983, Katula 1983, Mayes and Walker 1984, Cote et al 1985, Vanderbilt and Anderson 1985, Roth et al 1987, Schulman ct al. 1987.…”

Section: Hmgdmentioning

confidence: 99%

Histone variants and high mobility group non‐histone chromosomal proteins of higher plants: Their potential for forming a chromatin structure that is either poised for transcription or transcriptionally inert

Spiker

1988

Physiologia Plantarum

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In order for the genes of higher plants to be transcribed, they must be in a transcriptionally poised chromatin structure – a structure that allows access of RNA polymerases and transcription factors to the DNA. The structural features of transcriptionally poised chromatin and what distinguishes it from transcriptionally incrt chromatin are as yet unknown. There are, however, two groups of proteins that have been implicated as determinants of such divergent chromatin structures – the high mobility group (HMG) non‐histone chromatin proteins and histone variants. In this paper I discuss what is known of these two groups of proteins in higher plants against the background of their suspected roles in chromatin structure in animal systems. Plants have a number of histone variants (particularly of the H2A and H2B histones) which have the potential to be the basis of nucleosome heterogeneity in divergent chromatin structures. There is a large body of evidence from animal systems suggesting that HMG proteins are structural proteins of transcriptionally poised chromatin. Plants have non‐histone chromosomal proteins that can be defined as HMG proteins based on operational criteria. That is, they are extracted from purified chromatin with 0.35 M NaCl, are soluble in 2% trichloroacetie acid and are very highly charged proteins with their charges being about evenly split between basic and acidic amino acid residues. Characterization of the plant HMG proteins by overall amino acid composition, peptide mapping, partial sequencing and immunological cross reactivity indicates that the plant HMG proteins are very different from their putative animal counterparts. Nevertheless, plant HMG proteins bind to monoucleosomes in the same manner as animal HMG proteins; they are released from chromatin by mild DNase I (EC 3.1.4.5) digestion under conditions that lead to preferential digestion of transcriptionally active sequences; and when chromatin is separated into fractions enriched or depleted in transcribed DNA sequences, the plant HMG proteins are found in the fraction enriched in transcribed sequences.

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Section: Hmgdmentioning

confidence: 99%

Histone variants and high mobility group non‐histone chromosomal proteins of higher plants: Their potential for forming a chromatin structure that is either poised for transcription or transcriptionally inert

Spiker

1988

Physiologia Plantarum

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“…To identify most of the proteins in SDS/polyacrylamide gels that are modified by ADP-ribosylation, we also extracted HMG-like proteins (Cote et al, 1985) and analysed them for ADP-ribosylation. We could show that besides H1, which is co-extracted with the HMGlike proteins, all four HMG-like proteins (AS 1-4) are ADP-ribosylated ( Fig.…”

Section: Characterization Of Adprt Enzyme Formsmentioning

confidence: 99%

ADP-ribosylation in isolated nuclei of Physarum polycephalum

Golderer¹,

Schneider

Auer

et al. 1988

Biochemical Journal

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ADP-ribosylation of histones and non-histone nuclear proteins was studied in isolated nuclei during the naturally synchronous cell cycle of Physarum polycephalum. Aside from ADP-ribosyltransferase (ADPRT) itself, histones and high mobility group-like proteins are the main acceptors for ADP-ribose. The majority of these ADP-ribose residues is NH2OH-labile. ADP-ribosylation of the nuclear proteins is periodic during the cell cycle with maximum incorporation in early to mid G2-phase. In activity gels two enzyme forms with Mr of 115,000 and 75,000 can be identified. Both enzyme forms are present at a constant ratio of 3:1 during the cell cycle. The higher molecular mass form cannot be converted in vitro to the low molecular mass form, excluding an artificial degradation during isolation of nuclei. The ADPRT forms were purified and separated by h.p.l.c. The low molecular mass form is inhibited by different ADPRT inhibitors to a stronger extent and is the main acceptor for auto-ADP-ribosylation. The high molecular mass form is only moderately auto-ADP-ribosylated.

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“…The HI region in acid-urea gels is further contaminated with a protein, which is well separated from HI in the SDS gel. We named this band PX; this band was not present in a previous study on HMG-like proteins in Physarum amoebae (Cote et al, 1985). PX is one of the most abundant spots on Commassie Blue stained gels.…”

Section: Resultsmentioning

confidence: 90%

“…The low lysine content is reflected in the relatively weak label of this protein (in relation to its abundance) in fluorograms of two-dimensional gels. On the other hand, the mean content of glutamic acid and aspartic acid of AS1-4 was determined to be 21.30%, the mean content of basic amino acids 23.20%, and the lysine/arginine ratio 4.55 (Cote et al, 1985). It is therefore unlikely that protein PX represents another HMG-like protein in Physarum plasmodia.…”

Section: Resultsmentioning

confidence: 92%

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Periodic fluctuations of nuclear high-mobility-group-like proteins during the cell cycle of Physarum polycephalum

Smolarz

Gröbner²,

Loidl³

1988

Biochemistry

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High mobility group like (HMG-like) nuclear proteins were isolated from plasmodia of the lower eucaryote Physarum polycephalum and characterized by different types of polyacrylamide gel electrophoresis. The synthesis of these proteins was measured during the naturally synchronous cell cycle of Physarum. The four HMG-like proteins (AS1-4) exhibit a pronounced cell cycle dependent pattern of synthesis: AS1 and AS4 have a clear maximum of synthesis in mid S phase with a basal synthesis during the entire G2 period. In contrast, AS2 and AS3 have little synthesis in S phase but a broad maximum in mid G2 period. The four HMG-like proteins have a very low synthesis in early S phase and late G2 period. In addition, other non-histone proteins, which are coextracted with the HMG proteins, exhibit distinct periodic synthesis patterns. A novel non-histone protein, which is the most abundant protein species in 0.35 M NaCl extracts, was detected. It exhibits a high rate of synthesis around the time of mitosis. In general, the results indicate that, in contrast to the main cytoplasmic proteins, most nuclear proteins are phase-specific with respect to their synthesis in the cell cycle.

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High mobility group like chromosomal proteins from amebas of the acellular slime mold Physarum polycephalum

Cited by 8 publications

References 38 publications

Histone variants and high mobility group non‐histone chromosomal proteins of higher plants: Their potential for forming a chromatin structure that is either poised for transcription or transcriptionally inert

Histone variants and high mobility group non‐histone chromosomal proteins of higher plants: Their potential for forming a chromatin structure that is either poised for transcription or transcriptionally inert

ADP-ribosylation in isolated nuclei of Physarum polycephalum

Periodic fluctuations of nuclear high-mobility-group-like proteins during the cell cycle of Physarum polycephalum

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