A class of membrane proteins with a C-terminal anchor.

نویسندگان

  • U Kutay
  • E Hartmann
  • T A Rapoport
چکیده

Integral membrane proteins are generally targeted to translocation-competent membranes by virtue of signal sequences located close to the N-terminus of the polypeptide chain. Membrane anchoring is caused by the signal sequence or other hydrophobic segments located after it in the amino acid sequence. However, some integral membrane proteins do not follow these rules. The members of one class of nonconformist membrane proteins have no signal sequence, but instead possess a hydrophobic segment near the C-terminus that orients them with their N-termini in the cytoplasm. Members of this class are found in many organelles and are probably inserted into membranes by an unusual mechanism.

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

Transposition of domains between the M2 and HN viral membrane proteins results in polypeptides which can adopt more than one membrane orientation

The influenza A virus M2 polypeptide is a small integral membrane protein that does not contain a cleaved signal sequence, but is unusual in that it assumes the membrane orientation of a class I integral membrane protein with an NH2-terminal ectodomain and a COOH-terminal cytoplasmic tail. To determine the domains of M2 involved in specifying membrane orientation, hybrid genes were constructed ...

متن کامل

Immunogenic and Protective Potentials of Recombinant Receptor Binding Domain and a C-Terminal Fragment of Clostridium botulinum Neurotoxin Type E

Clostridium Botulinum Type E neurotoxin heavy chain consists of two domains: the translocation domain asthe N-terminal half and the binding domain as the Cterminal half (Hc). One effective way to neutralize botulinum neurotoxin is to inhibit binding of this toxin to neuromuscular synapses with antibodies against binding domain. Two synthetic genes, coding for Hc (the full length binding d...

متن کامل

Membrane insertion and intracellular transport of yeast syntaxin Sso2p in mammalian cells.

Proteins of the syntaxin family are suggested to play a key role in determining the specificity of intracellular membrane fusion events. They belong to the class of membrane proteins which are devoid of N-terminal signal sequence and have a C-terminal membrane anchor. Sso2p is a syntaxin homologue involved in the Golgi to plasma membrane vesicular transport in yeast. The protein was transiently...

متن کامل

Membrane topology of the Streptomyces lividans type I signal peptidases.

Most bacterial membranes contain one or two type I signal peptidases (SPases) for the removal of signal peptides from export proteins. For Streptomyces lividans, four different type I SPases (denoted SipW, SipX, SipY, and SipZ) were previously described. In this communication, we report the experimental determination of the membrane topology of these SPases. A protease protection assay of SPase...

متن کامل

Functions of signal and signal-anchor sequences are determined by the balance between the hydrophobic segment and the N-terminal charge.

The signal sequence of secretory proteins and the signal-anchor sequence of type II membrane proteins initiate the translocation of the following polypeptide segments, whereas the signal-anchor sequence of cytochrome P-450-type membrane proteins mediates the membrane insertion of the polypeptide via a signal-recognition particle-dependent mechanism but does not lead to the translocation of the ...

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:
  • Trends in cell biology

دوره 3 3  شماره 

صفحات  -

تاریخ انتشار 1993