An alternative procedure for the isolation of high mobility group proteins

Bhullar, Balwant S.; Candido, E. P. M.

doi:10.1016/0003-2697(81)90186-x

Cited by 11 publications

(3 citation statements)

References 7 publications

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“…Protein analysis was carried out as described by Lowry et al (1951). Extraction of HMG-like proteins from isolated nuclei followed published procedures (Goodwin et al, 1973;Bhullar & Candido, 1981). Fluorograms and autoradiograms were evaluated by densitometry using a Beckman DU-8B spectrophotometer with gel-scanning equipment.…”

Section: Other Methodsmentioning

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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Section: Other Methodsmentioning

confidence: 99%

ADP-ribosylation in isolated nuclei of Physarum polycephalum

Golderer¹,

Schneider

Auer

et al. 1988

Biochemical Journal

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“…The HMG proteins are extracted from chromatin or nuclei using either 0.35 M NaCl or perchloric acid, and then recovered from the extract by fractional precipitation with trichloroacetic acid, acetone (see [l]) or ammonium sulphate [13]. When this procedure was applied to the nuclei of P. polycephalum we obtained a fraction of proteins, which followed the extractability properties of the HMG proteins.…”

Section: Dnase I Digestion Of Nucleimentioning

confidence: 99%

HMG‐like proteins of Physarum polycephalum: Association with the transcriptionally active chromatin

Czupryn

Toczko

1984

FEBS Letters

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HMG-like proteins were isolated from nuclei of the acellular slime mold Physarum polycephalum. These proteins represented 0.6 + 0.2% of nuclear proteins and approx. 6% of DNA by weight. Polyacrylamide gel electrophoresis demonstrated the presence of 3 major proteins, designated HMG-lP, HMG-2P and HMG-14/17P. None of these proteins comigrated with any of the calf thymus HMGs. Physarum HMG-like proteins were found to be preferentially associated with transcriptionally active chromatin fraction, as well as being released from nuclei by light DNase I digestion, In contrast, the content of histone Hl was significantly lower in active than in inactive chromatin fraction. Physarum polycephalumHigh mobility group protein Transcriptionally active chromatin

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“…Extraction of HMG-like proteins was performed following published procedures (Goodwin et al, 1973;Bhullar & Candido, 1981). Isolated nuclei were resuspended in extraction buffer (0.35 M NaCl, 10 mM Tris-HCl,1 pH 7.5) and stirred on ice for 15 min.…”

Section: Methodsmentioning

confidence: 99%

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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An alternative procedure for the isolation of high mobility group proteins

Cited by 11 publications

References 7 publications

ADP-ribosylation in isolated nuclei of Physarum polycephalum

ADP-ribosylation in isolated nuclei of Physarum polycephalum

HMG‐like proteins of Physarum polycephalum: Association with the transcriptionally active chromatin

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

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