Characterization of the PL-I-related SP2 protein from Xenopus.
Biochemistry
; 46(44): 12700-8, 2007 Nov 06.
Article
em En
| MEDLINE
| ID: mdl-17927216
ABSTRACT
The complete cDNA sequence of Xenopus laevis sperm specific proteins SP1 and SP2 has been determined. This information when taken together with N-terminal sequencing and mass spectroscopy data indicates that these two proteins share a product precursor relationship in which SP2 results from cleavage of a short N-terminal peptide of SP1. The secondary and tertiary structures of SP2 have been characterized using circular dichroism and three dimension structure prediction. These structural analyses have conclusively shown that SP1/SP2 proteins are related to proteins of the histone H1 family, particularly to vertebrate histone H1x. Hence, they can be considered bona fide members of the protamine-like- I (PL-I) group of sperm nuclear basic proteins (SNBPs) that have been described in other vertebrate and invertebrate groups. SP2 binds to nucleosomal DNA in a way that is very similar to that of histone H1. However, its interaction with circular DNA does not exhibit an enhanced preference for the supercoiled conformation, and it appears to be mainly driven by ionic interactions.
Buscar no Google
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Xenopus
/
Fator de Transcrição Sp2
Tipo de estudo:
Prognostic_studies
Limite:
Animals
Idioma:
En
Ano de publicação:
2007
Tipo de documento:
Article