The developmentally regulated Drosophila embryonic nuclear lamina protein 'Young Arrest' (fs(1)Ya) is capable of associating with chromatin.

نویسندگان

  • J M Lopez
  • M F Wolfner
چکیده

The Drosophila fs(1)Ya protein (YA) is an essential component of the early embryonic nuclear lamina. Mutant zygotes lacking functional YA arrest in the first division cycles following fertilization, hence having a 'Young Arrest' of their development. The nuclear lamina is thought to act as the structural backbone for the nucleus and to provide anchoring sites for interphase chromosomes. Here, we demonstrate in vitro that YA is not required for the de novo formation of nuclear structures. Since YA's sequence predicts potential DNA binding motifs, this protein may instead function to connect the lamina and chromosomes, and thus aid in organizing the nucleus. We ectopically expressed YA in polytene cells and demonstrated its association with polytene chromosomes, preferentially at interbands. Furthermore, our in vitro studies indicate that embryonic YA protein is capable of associating with decondensed chromatin. These observations suggest that YA may be required for the interaction between chromatin and the nuclear envelope during early embryogenesis.

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 Drosophila nuclear lamina protein YA binds to DNA and histone H2B with four domains.

Dramatic changes occur in nuclear organization and function during the critical developmental transition from meiosis to mitosis. The Drosophila nuclear lamina protein YA binds to chromatin and is uniquely required for this transition. In this study, we dissected YA's binding to chromatin. We found that YA can bind to chromatin directly and specifically. It binds to DNA but not RNA, with a pref...

متن کامل

DNA Sequence-Dependent Compartmentalization and Silencing of Chromatin at the Nuclear Lamina

A large fraction of the mammalian genome is organized into inactive chromosomal domains along the nuclear lamina. The mechanism by which these lamina associated domains (LADs) are established remains to be elucidated. Using genomic repositioning assays, we show that LADs, spanning the developmentally regulated IgH and Cyp3a loci contain discrete DNA regions that associate chromatin with the nuc...

متن کامل

Nuclear Architecture and Epigenetics of Lineage Choice

Differentiation is an epigenetic process which is installed by changes of transcriptional programs over successive cellular divisions. A number of studies have reported the effects of biochemical modifications of chromatin (DNA and chromatin proteins) on the regulation of transcription. Although, these studies are able to explain how transcription of a given gene is regulated (toward activation...

متن کامل

A hydrophilic lamin-binding domain from the Drosophila YA protein can target proteins to the nuclear envelope.

The nuclear lamina provides an architectural framework for the nuclear envelope and an attachment site for interphase chromatin. In Drosophila eggs and early embryos its major constituent, lamin Dm0, interacts with a lamina protein called YA. When the lamin-interaction region of YA is deleted, YA still enters nuclei but fails to localize to nuclear envelopes, suggesting that lamin interaction t...

متن کامل

Lamin activity is essential for nuclear envelope assembly in a Drosophila embryo cell-free extract

The role of the Drosophila lamin protein in nuclear envelope assembly was studied using a Drosophila in vitro assembly system that reconstitutes nuclei from added sperm chromatin or naked DNA. Upon incubation of the embryonic assembly extract with anti-Drosophila lamin antibodies, the attachment of nuclear membrane vesicles to chromatin surface and nuclear envelope formation did not occur. Lami...

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:
  • Journal of cell science

دوره 110 ( Pt 5)  شماره 

صفحات  -

تاریخ انتشار 1997