MODIFICATION OF HISTONES BY THE SUGAR β-N-ACETYLGLUCOSAMINE (GlcNAc) OCCURS ON MULTIPLE RESIDUES, INCLUDING H3 SERINE 10, AND IS CELL CYCLE REGULATED

نویسندگان

  • Suisheng Zhang
  • Kevin Roche
  • Heinz-Peter Nasheuer
  • Noel Francis Lowndes
چکیده

1 MODIFICATION OF HISTONES BY THE SUGAR β-N-ACETYLGLUCOSAMINE (GlcNAc) OCCURS ON MULTIPLE RESIDUES, INCLUDING H3 SERINE 10, AND IS CELL CYCLE REGULATED Suisheng Zhang, Kevin Roche, Heinz-Peter Nasheuer, and Noel Francis Lowndes* Genome Stability Laboratory & Cell Cycle Control Laboratory, Center for Chromosome Biology, National University of Ireland Galway, University Road, Galway, Ireland Running title: Histone O-GlcNAcylation in the cell cycle *Address for correspondence: Noel F. Lowndes, Genome Stability Laboratory, Center for Chromosome Biology, National University of Ireland Galway, University Road, Galway, Ireland Phone: 00 353 91 492415; E-mail: [email protected] Abbreviations: O-GlcNAcylation, phosphorylation, histones, cell cycle.

برای دانلود 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

O-GlcNAc-Specific Antibody CTD110.6 Cross-Reacts with N-GlcNAc2-Modified Proteins Induced under Glucose Deprivation

Modification of serine and threonine residues in proteins by O-linked β-N-acetylglucosamine (O-GlcNAc) glycosylation is a feature of many cellular responses to the nutritional state and to stress. O-GlcNAc modification is reversibly regulated by O-linked β-N-acetylglucosamine transferase (OGT) and β-D-N-acetylglucosaminase (O-GlcNAcase). O-GlcNAc modification of proteins is dependent on the con...

متن کامل

The role of intracellular protein O-glycosylation in cell adhesion and disease☆

Post-translational protein modification, including phosphorylation, is generally quick and reversible, facilitating rapid biologic adjustments to altered cellular physiologic demands. In addition to protein phosphorylation, other post-translational modifications have been identified. Intracellular protein O-glycosylation, the addition of the simple sugar O-linked N-acetylglucosamine (O-GlcNAc) ...

متن کامل

Detecting O-GlcNAc using in vitro sulfation.

O-linked β-N-acetylglucosamine (O-GlcNAc) glycosylation, the covalent attachment of N-acetylglucosamine to serine and threonine residues of proteins, is a post-translational modification that shares many features with protein phosphorylation. O-GlcNAc is essential for cell survival and plays important role in many biological processes (e.g. transcription, translation, cell division) and human d...

متن کامل

O-GlcNAcase Expression is Sensitive to Changes in O-GlcNAc Homeostasis

O-linked N-acetylglucosamine (O-GlcNAc) is a post-translational modification involving an attachment of a single β-N-acetylglucosamine moiety to serine or threonine residues in nuclear and cytoplasmic proteins. Cellular O-GlcNAc levels are regulated by two enzymes: O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA), which add and remove the modification, respectively. The levels of O-GlcNAc can r...

متن کامل

Developmental Regulation of Protein O-GlcNAcylation, O-GlcNAc Transferase, and O-GlcNAcase in Mammalian Brain

O-GlcNAcylation is a common posttranslational modification of nucleocytoplasmic proteins by β-N-acetylglucosamine (GlcNAc). The dynamic addition and removal of O-GlcNAc groups to and from proteins are catalyzed by O-linked N-acetylglucosamine transferase (O-GlcNAc transferase, OGT) and β-N-acetylglucosaminidase (O-GlcNAcase, OGA), respectively. O-GlcNAcylation often modulates protein phosphoryl...

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

برای دانلود 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

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2011