Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/3919
Title: Molluscan sperm proteins: Ensis minor
Authors: Giancotti, V
Buratti, E
Santucci, Annalisa 
Neri, Paolo
Crane Robinson, C.
Issue Date: 1992
Project: None 
Journal: BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY
Abstract: 
The three major proteins, EM1, EM5 and EM6, from the mature sperm of the bivalve mollusc Ensis minor have been partially sequenced in order to establish which category they belong to and their potential for phosphorylation. Protein EM1 is protamine-like with about 50% basic amino acids, some of which are included in SK(R) repeats. Three SPXX potential phosphorylation sites were observed in the N-terminal domain. EM1 does not fold (Giancotti et al. (1983) Eur. J. Biochem. 136, 509-516). Protein EM6 (approx. 270 residues) is histone H1-like, having a globular domain homologous to other H1 family proteins. The N-domain of EM6 contains SK(R) repeats like EM1, but there are few, if any, SPXX sites in the chain. Proteins EM1 and EM6 are the two proteins specific for mature sperm. Protein EM5, of about 150 residues and present at lower levels than EM1 and EM6, is also an H1-family molecule. A sequence from its globular domain shows close homology to chicken H5 and to sea urchin somatic H1. Its presence may relate to the existence of a low level of nucleosomal structure.
Description: 
24698
URI: http://hdl.handle.net/20.500.12779/3919
ISSN: 0167-4838
DOI: 10.1016/0167-4838(92)90217-2
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