The primary structure of non-histone chromosomal protein HMG17 from chicken erythrocyte nuclei.

نویسندگان

  • J M Walker
  • C Stearn
  • E W Johns
چکیده

Chromatin contains a group of non-histone proteins called the high mobility group (HMG) proteins (reviewed [l]). There are 4 main HMG proteins in calf thymus, HMG 1,2, 14 and 17, which have all been shown to be present in isolated nucleosomes [2]. Some minor HMG protein components of calf thymus chromatin have also been characterised [3]. Attention has been focused on HMG14 and 17 because of their possible role in gene transcription [4,5]. The complete amino acid sequences of calf thymus HMG14 and 17 have been determined [6,7] and partial sequences are available for HMG1 and 2 [ 1,8]. HMG proteins have been shown to be present in a variety of organisms and tissues, including avian erythrocytes [9,10] trout testis and liver [11,12] and wheat and yeast [ 131 but little is known about the structures of the HMG proteins from these sources. One of the questions that needs to be answered concerning the HMG proteins is whether they exhibit the same extreme evolutionary stability as shown by the nucleosome core histones. As part of a programme of study on the structure of HMG proteins from various species we have now determined the complete amino acid sequence of HMG17 from chicken erythrocyte nuclei.

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

The effect of aspirin on the interaction of histone 05 and 05-DNA

The linker histones (H1 or H5) which play a key role in the folding of chromatin, are general repressors of gene expression. Nuclei of the mature chicken erythrocytes (and in some mammalian cells) contain both of them. Although the interaction of H5 with DNA is stronger than that of H1, it does not prevent the transcription of some erythroid-specific genes. It has been shown that some modificat...

متن کامل

Histone stoichiometry in chicken erythrocyte nuclei.

HISTONE STOICHIOMETRY IN CHICKEN ERYTHROCYTE NUCLEI Everline B. Wright and Donald E. Olins University of Tennessee-Oak Ridge Graduate School of Biomedical Sciences Biology Division, Oak Ridge National Laboratory Oak Ridge, Tennessee 37830 Received January 30,1975 SUM}{ARY: In order to establish a quantitative relationship among the major histone components in chicken erythrocyte nuclei, an elec...

متن کامل

Release of a globin gene enriched chromatin fraction from chicken erythrocyte nuclei following DNase II digestion.

Mild digestion of chicken erythrocyte nuclei with deoxyribonuclease II results in the release of a chromatin fraction which is 4- to 13-fold enriched for the globin coding sequences when compared to total chicken DNA. The remaining nuclear pellet is depleted in these sequences. A maximum of 25% of the globin genes have been recovered in the released fraction. The addition of 5 mM sodium butyrat...

متن کامل

Gene-specific differences in the aflatoxin B1 adduction of chicken erythrocyte chromatin.

Mature and immature chicken erythrocyte nuclei were treated with activated aflatoxin B1 (2,3-dichloroaflatoxin B1), producing covalently bound DNA adducts. This reaction produces alkali-labile sites in the DNA which can be identified by using a variation of the Maxam-Gilbert sequencing procedure. We determined the aflatoxin B1 accessibility of defined regions of the erythroid genome by using di...

متن کامل

Synthesis of high mobility group proteins in regenerating rat liver.

Incorporation of [3H]lysine into the non-histone chromosomal proteins HMG1, HMG2, and HMG17 and into each of the five major classes of histones was measured in rat liver at various times after partial hepatectomy. Histone synthesis was closely coupled temporally to that of DNA, although a small amount of histone was shown to be produced before DNA replication began. In contrast, the incorporati...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

عنوان ژورنال:
  • FEBS letters

دوره 112 2  شماره 

صفحات  -

تاریخ انتشار 1980