Extraction and Characterization of the Phenol-Soluble Acidic Nuclear Proteins

1974 ◽  
pp. 59-102 ◽  
Author(s):  
WALLACE M. LESTOURGEON ◽  
WAYNE WRAY
Keyword(s):  
Nuclear Proteins

Characterization of Zn2+-binding nuclear proteins present in the myocardium

1993 ◽  
Vol 121 (2) ◽  
pp. 175-179 ◽  
Author(s):  
Choong-Chin Liew ◽  
Eva Cukerman
Keyword(s):  
Nuclear Proteins

Characterization of SERCA2b Ca2+–Mg2+ ATPase mRNA decay by nuclear proteins

Cell Calcium ◽  
2007 ◽  
Vol 41 (6) ◽  
pp. 581-592 ◽  
Author(s):  
Tao Chen ◽  
Paromita Ghosh ◽  
Christine M. Misquitta ◽  
Archana Govindan ◽  
Ashok K. Grover
Keyword(s):  
Mrna Decay ◽  
Nuclear Proteins

THE BASIC PROTEINS OF TROUT TESTIS CHROMATIN: ASPECTS OF THEIR SYNTHESIS, POST-SYNTHETIC MODIFICATIONS AND BINDING TO DNA

1972 ◽  
Vol 71 (2_Suppla) ◽  
pp. S130-S154 ◽  
Author(s):  
Gordon H. Dixon
Keyword(s):  
Developmental Changes ◽  
Nuclear Proteins ◽  
Velocity Sedimentation ◽  
Primary Sequence ◽  
Volume Changes ◽  
Basic Proteins ◽  
Isolation And Characterization ◽  
Pass Through

ABSTRACT Spermatogenesis in rainbow trout provides a favourable system for the study of the striking changes in the population of basic nuclear proteins in the chromatin of the developing sperm. Methods are described for the isolation and characterization of the basic proteins of testis both on the preparative and the micro-scale. Large volume changes occur as cells pass through the series of developmental changes and they may be readily separated by velocity sedimentation at one gravity. This enables a study to be made of the timing of particular biochemical events during development. The process whereby the histones are removed and replaced by newly synthesized protamines is examined in detail and possible mechanisms discussed. The role of post-synthetic modification of basic proteins by phosphorylation and acetylation is examined and the sites of these modifications in the primary sequence of protamine and histones determined. From a study of the timing of the modification reactions, it appears that phosphorylation and acetylation play an important role in modulating the correct binding of highly basic regions of histones to DNA while acetylation may also be involved in de-stabilizing the tight complexes between DNA and the basic NH2-terminal regions of histones IIb1, IIb2, III and IV as a preliminary to their replacement by protamine and the formation of the very compact nucleo-protamine of the mature sperm.

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