Hydrophobic Labeling and Cross-Linking of Membrane Proteins

1982 ◽  
pp. 173-184 ◽  
Author(s):  
Hans Sigrist ◽  
Peter Zahler
Keyword(s):  
Membrane Proteins ◽  
Cross Linking

scholarly journals Glycan-protein cross-linking mass spectrometry reveals sialic acid-mediated protein networks on cell surfaces

2021 ◽  
Author(s):  
Yixuan Xie ◽  
Siyu Chen ◽  
Qiongyu Li ◽  
Ying Sheng ◽  
Michael R Alvarez ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Sialic Acid ◽  
Membrane Proteins ◽  
Cell Membranes ◽  
Sialic Acids ◽  
Cross Linking ◽  
Protein Networks ◽  
Cell Surfaces ◽  
Protein Cross Linking

A cross-linking method is developed to elucidate the glycan-mediated interactions between membrane proteins through sialic acids. The method provides previously unknown extensive glycomic interactions on cell membranes. The vast majority...

Coupling of amines to and cross-linking of endogenous cytosol or membrane proteins by hepatic transglutaminase

1979 ◽  
Vol 28 (10) ◽  
pp. 1601-1608 ◽  
Author(s):  
Ilona Linnoila ◽  
Takashi Abe ◽  
Peter Voytek ◽  
Richard P. Diaugustine
Keyword(s):  
Membrane Proteins ◽  
Cross Linking

scholarly journals Identification of Protein Transport Complexes in the Chloroplastic Envelope Membranes via Chemical Cross-Linking

1997 ◽  
Vol 136 (5) ◽  
pp. 983-994 ◽  
Author(s):  
Mitsuru Akita ◽  
Erik Nielsen ◽  
Kenneth Keegstra
Keyword(s):  
Membrane Proteins ◽  
Protein Transport ◽  
Protein Import ◽  
Cross Linking ◽  
Envelope Membrane ◽  
Precursor Proteins ◽  
Intact Chloroplasts ◽  
Outer Envelope Membrane ◽  
Envelope Membranes ◽  
Chemical Cross Linking

Transport of cytoplasmically synthesized proteins into chloroplasts uses an import machinery present in the envelope membranes. To identify the components of this machinery and to begin to examine how these components interact during transport, chemical cross-linking was performed on intact chloroplasts containing precursor proteins trapped at a particular stage of transport by ATP limitation. Large crosslinked complexes were observed using three different reversible homobifunctional cross-linkers. Three outer envelope membrane proteins (OEP86, OEP75, and OEP34) and one inner envelope membrane protein (IEP110), previously reported to be involved in protein import, were identified as components of these complexes. In addition to these membrane proteins, a stromal member of the hsp100 family, ClpC, was also present in the complexes. We propose that ClpC functions as a molecular chaperone, cooperating with other components to accomplish the transport of precursor proteins into chloroplasts. We also propose that each envelope membrane contains distinct translocation complexes and that a portion of these interact to form contact sites even in the absence of precursor proteins.

scholarly journals YidC Occupies the Lateral Gate of the SecYEG Translocon and Is Sequentially Displaced by a Nascent Membrane Protein

2013 ◽  
Vol 288 (23) ◽  
pp. 16295-16307 ◽  
Author(s):  
Ilie Sachelaru ◽  
Narcis Adrian Petriman ◽  
Renuka Kudva ◽  
Patrick Kuhn ◽  
Thomas Welte ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Membrane Protein ◽  
Lipid Bilayer ◽  
Transmembrane Domains ◽  
Cross Linking ◽  
Lipid Phase ◽  
Lipid Transfer ◽  
Lateral Gate

Most membrane proteins are co-translationally inserted into the lipid bilayer via the universally conserved SecY complex and they access the lipid phase presumably via a lateral gate in SecY. In bacteria, the lipid transfer of membrane proteins from the SecY channel is assisted by the SecY-associated protein YidC, but details on the SecY-YidC interaction are unknown. By employing an in vivo and in vitro site-directed cross-linking approach, we have mapped the SecY-YidC interface and found YidC in contact with all four transmembrane domains of the lateral gate. This interaction did not require the SecDFYajC complex and was not influenced by SecA binding to SecY. In contrast, ribosomes dissociated the YidC contacts to lateral gate helices 2b and 8. The major contact between YidC and the lateral gate was lost in the presence of ribosome nascent chains and new SecY-YidC contacts appeared. These data demonstrate that the SecY-YidC interaction is influenced by nascent-membrane-induced lateral gate movements.

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