Biomedical subjects
Publications and source records attributed to C Von Holt.
A 46 kDa ATP binding polypeptide of the nuclear envelope, virtually identical to the nuclear envelope NTPase putatively involved in mRNA efflux [6], is present in all rat liver cell membranes. Its presence in nuclear envelope is not the result of cross contamination during isolation.
The histone H2A(2) type from wheat germ comprises at least two highly homologous isohistones with 151 amino acid residues. Microheterogeneity occurs mainly at the N-terminal and C-terminal regions. These isohistones have both N-terminal (7 amino acid residues) and C-terminal (15 amino acid residues) extensions relative to calf thymus histone H2A.
A hybrid histone octamer was reconstituted from erythrocyte H2A and H2B, avian [110 Cys-des-thio]histone H3 and the sea-urchin sperm [73Cys]H4 variant. [110Cys-Des-thio]histone H3 was prepared by reaction of natural H3 with Raney nickel. The ability of the hybrid octamer to crystallize to the same form as the natural octamer demonstrated that the chemical modification of cysteine to alanine in H3 and the mutation from threonine to cysteine in sperm H4 do not alter histone-histone interactions in the octamer. Since the sulfhydryl groups of both H4 molecules are fully accessible to 5,5'-dithiobis(2-nitrobenzoate) these residues provide suitable sites for the introduction of a single cysteine-specific label per H4 molecule in the octamer.
The histone H1 fraction from gastrula of the sea urchin Parechinus angulosus consists of a multitude of polypeptides with different electrophoretic mobilities. The synthesis of these proteins is programmed. Amino acid composition, electrophoretic properties and sequence homologies identify these as isohistones H1. One of these isohistones atypically binds the non-ionic detergent Triton X-100.
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The primary structure of the amino-terminal 84 residues of sperm histone H1Parechinus has been determined. The sequence is: Pro-Gly-Ser-Pro-Gln-Lys-Arg-Ala-Ala-Ser-Pro-Arg-Lys-Ser-Pro-Arg-Lys-Ser-Pro-Lys-Lys-Ser-Pro-Arg-Lys-Ala-Ser-Ala-Ser-Pro-Arg-Arg-Lys-Ala-Lys-Arg-Ala-Arg-Ala-Ser-Thr-His-Pro-Pro-Val-Leu-Glu-Met-Val-Gln-Ala-Ala-Ile-Thr-Ala-Met-Lys-Glu-Arg-Lys-Gly-Ser-Ser-Ala-Ala-Lys-Ile-Lys-Ser-Tyr-Met-Ala-Ala-Asn-Tyr-Arg-Val-Asp-Met-Asn-Val-Leu-Ala-Pro-.
The primary structure of sperm histone H1Parechinus has been determined. H1Parechinus consists of a polypeptide chain of the following 248 amino acid residues: Pro-Gly-Ser-Pro-Gln-Lys-Arg-Ala-Ala-Ser-Pro-Arg-Lys-Ser-Pro-Arg-Lys-Ser-Pro-Lys-Lys-Ser-Pro-Arg-Lys-Ala-Ser-Ala-Ser-Pro-Arg-Arg-Lys-Ala-Lys-Arg-Ala-Arg-Ala-Ser-Thr-His-Pro-Pro-Val-Leu-Glu-Met-Val-Gln-Ala-Ala-Ile-Thr-Ala-Met-Lys-Glu-Arg-Lys-Gly-Ser-Ser-Ala-Ala-Lys-Ile-Lys-Ser-Tyr-Met-Ala-Ala-Asn-Tyr-Arg-Val-Asp-Met-Asn-Val-Leu-Ala-Pro-His-Val-Arg-Arg-Ala-Leu-Arg-Asn-Gly-Val-Ala-Ser-Gly-Ala-Leu-Lys-Gln-Val-Thr-Gly-Thr-Gly-Ala-Ser-Gly-Arg-Phe-Arg-Val-Gly-Ala-Val-Ala-Lys-Pro-Lys-Lys-Ala-Lys-Lys-Thr-Ser-Ala-Ala-Ala-Lys-Ala-Lys-Lys-Ala-Lys-Ala-Ala-Ala-Ala-Lys-Lys-Ala-Arg-Arg-leads to Lys-Ala-Lys-Ala-Ala-Ala-Lys-Arg-Lys-Ala-Ala-Leu-Ala-Lys-Lys-Lys-Ala-Ala-Ala-Ala-Lys-Arg-Lys-Ala-Ala-Ala-Lys-Ala-Lys-Lys-Ala-Lys-Lys-Pro-Lys-Lys-Lys-Ala-Ala-Ala-Lys-Lys-Ala-Lys-Lys-Pro-Ala-Lys-Lys-Ser-Pro-Lys-Lys-Ala-Lys-Lys-Pro-Ala-Lys-Lys-Ser-Pro-Lys-Lys-Lys-Lys-Ala-Lys-Arg-Ser-Pro-Lys-Lys-Ala-Lys-Lys-Ala-Ala-Gly-Lys-Arg-Lys-Pro-Ala-Ala-Lys-Lys-Ala-Arg-Arg-Ser-Pro-Arg-Lys-Ala-Gly-Lys-Arg-Arg-Ser-Pro-Lys-Lys-Ala-Arg-Lys. The protein consists of three domains. Compared to other H1 and H5 histones, there is a very similar hydrophobic central domain and the carboxyl-terminal domain is very rich in lysine and alanine. H1Parechinus is similar to H5 histones in that the carboxyl-terminal domain also contains many arginine residues close to the carboxyl terminus. The carboxyl-terminal domain of H1Parechinus appears to have been constructed by a series of variable duplications. The amino-terminal domain of H1Parechinus is longer and quire different to that of other H1 and H5 histones and is characterized by a repeating tetrapeptide of the general type Ser-Pro-(basic)2. The known sequence of a histone H1 gene from Psammechinus miliaris [Schaffner, W. et al. (1978) Cell, 14, 655-671] is compared to the sequence of H1Parechinus. Again the central hydrophobic domains are similar whereas the amino terminal domains are very different. The functions of the various domains of sperm histone H1Parechinus are discussed.
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The primary structure of a third H2B histone isolated from sperm of the sea urchin Parechinus angulosus has been determined. H2B(3) consists of a polypeptide chain of the following 148 amino acid residues: Pro-Arg-Ser-Pro-Ala-Lys-Thr-Ser-Pro-Arg-Lys-Gly-Ser-Pro-Arg-Lys-Gly-Ser-Pro-Arg-Lys-Gly-Ser-Pro-Ser-Arg-Lys-Ala-Ser-Pro-Lys-Arg-Gly-Gly-Lys-Gly-Ala-Lys-Arg-Ala-Gly-Lys-Gly-Gly-Arg-Arg-Arg-Arg-Val-Val-Lys-Arg-Arg-Arg-Arg-Arg-Arg-Glu-Ser-Tyr-Gly-Ile-Tyr-Ile-Tyr-Lys-Val-Leu-Lys-Gln-Val-His-Pro-Asp-Thr-Gly-Ile-Ser-Ser-Arg-Ala-Met-Ser-Val-Met-Asn-Ser-Phe-Val-Asn-Asp-Val-Phe-Glu-Arg-Ile-Ala-Ser-Glu-Ala-Ser-Arg-Leu-Thr-Ser-Ala-Asn-Arg-Arg-Ser-Thr-Val-Ser-Ser-Arg-Glu-Ile-gln-Thr-Ala-Val-Arg-Leu-Leu-Leu-Pro-Gly-Glu-Leu-Ala-Lys-His-Ala-Val-Ser-Glu-Gly-Thr-Lys-Ala-Val-Thr-Lys-Tyr-Thr-Thr-Ser-Arg. H2B(3) Parechinus closely resembles HIB(2) Parechinus but has one additional repeating pentapeptide in the amino-terminal region and a serine replacing glycine at position 98.
Histones H2B have been isolated from the terminally differentiated diploid erythrocytes of three different classes, amphibia (Xenopus laevis), reptilia (Crocodilus niloticus) and aves (Gallus domesticus). Partial amino acid sequences revealed three regions of sequence variation, each variant involving a single amino acid substitution.
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It has been observed that proline residues often initiate overlaps during sequenator analysis. The cause has been shown to be an abnormally slow cleavage reaction. The kinetics of the cleavage reaction has been studied and found to obey pseudo-first-order kinetics. There are considerable differences in reaction rates depending on the position of proline in the sequence, as demonstrated for the four prolines in the N-terminal section of the H2B histone from chicken.
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