The Complete Amino‐Acid Sequence of Histone H2B(2) from Sperm of the Sea Urchin Parechinus angulosus
- 1 July 1977
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 77 (2) , 277-286
- https://doi.org/10.1111/j.1432-1033.1977.tb11666.x
Abstract
Sperm histone H2B(2)Parechinus consists of a single polypeptide chain of the following 143 amino acids: Pro‐Arg‐Ser‐Pro‐Ala‐Lys‐Thr‐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‐Gly‐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. In a previously published partial sequence positions 25, 34, 40 and 41 were incorrectly assigned.The amino‐terminal one third of sperm histone H2B(2)Parechinus is highly basic containing a repeating pentapeptide occurring over the first 24 residues. This repeating pentapeptide is different to that of sperm histone H2B(1)Parechinus. In this region there is very little amino acid sequence homology between H2B(1)Parechinus, H2B(2)Parechinus on the one side and H2Bcalf thymus on the other side, but all three proteins are highly basic in their N‐terminal parts.The carboxyl‐terminal two thirds of sperm histone H2B(2) is hydrophobic except for a short polar region of 20 amino acids. The carboxyl‐terminal region shows a very high amino acid sequence homology between the three H2B histones. Much of the variability occurs in the short polar region whereas the hydrophobic regions are almost completely constant. The majority of the amino acid substitutions that occur in the carboxyl end are conservative.The three H2B protein sequences are compared and the functional and evolutionary significance of the changes is discussed.This publication has 20 references indexed in Scilit:
- The Complete Amino‐Acid Sequence of Histone H2B(1) from Sperm of the Sea Urchin Parechinus angulosusEuropean Journal of Biochemistry, 1977
- Chromosomal Proteins and Chromatin StructureAnnual Review of Biochemistry, 1975
- Chicken erythrocyte histone H5; I amino terminal sequence (70 residues)FEBS Letters, 1975
- The Determination of the Primary Structure of Histone F3 from Chicken Erythrocytes by Automatic Edman DegradationEuropean Journal of Biochemistry, 1974
- Sequence of the cysteine‐containing portion of histone F2al from the sea urchin Parechinus angulosusFEBS Letters, 1974
- Comparison of the N‐terminal amino acid sequences of histone F3 from a mammal, a bird, a shark, an echinoderm, a mollusc and a plant.FEBS Letters, 1974
- Partial amino acid sequence of two new arginine—serine rich histones from male gonads of the sea urchin (Parechinus angulosus)FEBS Letters, 1974
- Oxidation of the cysteine-containing histone F3. Detection of an evolutionary mutation in a conservative histoneBiochemistry, 1971
- Planning Complex Building SystemsNature, 1971
- Amino-acid Sequence of Slightly Lysine-rich HistoneNature, 1970