Abstract
In <em>Chara tomentosa</em> during mid spermiogenesis (phases V, VI, VII) when the amount of nuclear protamine-type proteins increases, while the amount of histones decreases, in connection with chromatin remodelling, an extensive RER system filled with dark, fine-granular substance is observed. The intermembranous space of the nuclear envelope is filled with a homogenous substance which looks similar. The most extensive ER system can be observed in phase V, which is at the beginning of nuclear protein exchange. The results presented in this paper correspond with the earlier suggestion based on <em>Chara vulgaris</em> spermioge nesis studies, that ER takes part in a protamine-type protein synthesis, which enter a nucleus by endocytosis, through an inner nuclear envelope membrane.
Highlights
During spermiogenesis in animals, a dramatic remodelling of chromatin takes place, leading to extreme condensation connected with the replacement of histones with protamines or other more basic proteins (Wouters-Tyrou et al 1998; Steger 1999)
The studies have shown that a small amount of protamine-type protein appears in mid spermiogenesis, and reaches nearly a maximal level in late spermiogenesis
The present study has shown that this characteristic period occurs in C. tomentosa
Summary
A dramatic remodelling of chromatin takes place, leading to extreme condensation connected with the replacement of histones with protamines or other more basic proteins (Wouters-Tyrou et al 1998; Steger 1999). Capillar electrophoresis of mature spermatozoids of C. tomentosa has shown no histone proteins which are replaced with 3 fractions of basic proteins with electrophoretic mobility, similar to that of salmon protamines (Kamierczak 2000; Kwiatkowska et al 2002). The studies have shown that a small amount of protamine-type protein appears in mid spermiogenesis, and reaches nearly a maximal level in late spermiogenesis. It was observed that positive reaction to protamine-type proteins appeared in phase V, and gradually increased
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