Intramolecular chaperones: polypeptide extensions that modulate protein folding
Abstract
Several prokaryotic and eukaryotic proteins are synthesized as precursors in the form of pre-pro-proteins. While the pre-regions function as signal peptides that are involved in transport, the propeptides can often catalyze correct folding of their associated proteins. Such propeptides have been termed intramolecular chaperones. In cases where propeptides may not directly catalyze the folding reaction, it appears that they can facilitate processes such as structural organization and oligomerization, localization, sorting and modulation of enzymatic activity and stability of proteins. Based on the available literature it appears that propeptides may actually function as 'post-translational modulators' of protein structure and function. Propeptides can be classified into two broad categories: Class I propeptides that function as intramolecular chaperones and directly catalyze the folding reaction; and Class II propeptides that are not directly involved in folding.
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The prodomain of PrtB is a class I propeptide that confers a foldase activity sufficient for proteinase folding.
“This prompted us to propose the prodomain of PrtB as a class I propeptide that confers a foldase activity sufficient for proteinase folding (34).”
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Pohl, S., & Harwood, C. R. (2010) · Advances in applied microbiology · doi:10.1016/s0065-2164(10)73001-x · Cited by 115 · see citing works
The intramolecular chaperone-mediated protein folding
Chen, Y.-J., & Inouye, M. (2008) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2008.10.005 · Cited by 112 · see citing works
Self-citationFolding Pathway Mediated by an Intramolecular Chaperone
Yabuta, Y., Takagi, H., Inouye, M., & Shinde, U. P. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m107573200 · Cited by 104 · see citing works
Self-citationWaschkowitz, T., Rockstroh, S., & Daniel, R. (2009) · Applied and Environmental Microbiology · doi:10.1128/aem.02136-08 · Cited by 85 · see citing works
Hepatitis C virus NS2 is a protease stimulated by cofactor domains in NS3
Schregel, V., Jacobi, S., Pénin, F., & Tautz, N. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0810950106 · Cited by 81 · see citing works
“, subtilisin or -lytic protease) where they are called prosequences and precede the protease domain in the polypeptide chain (18).”
BackgroundFolding Pathway Mediated by an Intramolecular Chaperone
Fu, X., Inouye, M., & Shinde, U. P. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.22.16871 · Cited by 80 · see citing works
Self-citationProcessing of peptide and hormone precursors at the dibasic cleavage sites
Rholam, M., & Fahy, C. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0007-5 · Cited by 76 · see citing works
“Alternatively, the PCs recognize some regions of structure in addition to the single or paired basic residues [2, 22], or their actions may be directed by conformation of the processing domains which could focus the action of protease onto particular sites [20, 21].”
BackgroundThe role of the D1 domain of the von Willebrand factor propeptide in multimerization of VWF
Rosenberg, J. B., Haberichter, S. L., Jozwiak, M. A., Vokac, E., Kroner, P. A., Fahs, S. A., Kawai, Y., & Montgomery, R. R. (2002) · Blood · doi:10.1182/blood-2002-03-0789 · Cited by 75 · see citing works
Shinde, U. P., & Thomas, G. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-204-5_4 · Cited by 68 · see citing works
“In some cases propeptides are known to regulate different types of cellular processes such as transport and localization, hierarchical organization, or oligomerization and regulation of protein activity–function by indirectly modulating protein conformations and can be termed as “post-translational modulators” of prot…”
BackgroundInfluentialSelf-citationGerminants and Their Receptors in Clostridia
Bhattacharjee, D., McAllister, K. N., & Sorg, J. A. (2016) · Journal of Bacteriology · doi:10.1128/jb.00405-16 · Cited by 66 · see citing works
Gu, Z. C., & Enenkel, C. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1699-8 · Cited by 66 · see citing works
“In principle, the propeptides participate in protein folding and assist in b subunit incorporation [60].”
Demidyuk, I. V., Калашников, А. Е., Gromova, T. Y., Gasanov, E. V., Safina, D. R., Zabolotskaya, M. V., Rudenskaya, G. N., & Kostrov, S. V. (2006) · Protein Expression and Purification · doi:10.1016/j.pep.2005.12.005 · Cited by 62 · see citing works
Tanaka, S., Matsumura, H., Koga, Y., Takano, K., & Kanaya, S. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.07.027 · Cited by 59 · see citing works
Pandey, K. C., Sijwali, P. S., Singh, A., Na, B., & Rosenthal, P. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310536200 · Cited by 58 · see citing works
Sijwali, P. S., Shenai, B. R., & Rosenthal, P. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109680200 · Cited by 56 · see citing works
Sachkova, M. Y., Landau, M., Surm, J. M., Macrander, J., Singer, S. A., Reitzel, A. M., & Moran, Y. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2011120117 · Cited by 55 · see citing works
Houssen, W. E., Koehnke, J., Zollman, D., Vendôme, J., Raab, A., Smith, M. C. M., Naismith, J. H., & Jaspars, M. (2012) · ChemBioChem · doi:10.1002/cbic.201200661 · Cited by 53 · see citing works
Bacterial adhesins: structural studies reveal chaperone function and pilus biogenesis
Knight, S. D. (2000) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(00)00144-7 · Cited by 54 · see citing works
Yeung, P. S. M., Zagorski, N., & Marquis, H. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.8.2601-2608.2005 · Cited by 51 · see citing works
Propeptides as modulators of functional activity of proteases
Demidyuk, I. V., Shubin, A. V., Gasanov, E. V., & Kostrov, S. V. (2010) · BioMolecular Concepts · doi:10.1515/bmc.2010.025 · Cited by 48 · see citing works
Cynthia Marie-claire, A., Yabuta, Y., Suefuji, K., Matsuzawa, H., & Shinde, U. P. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.4233 · Cited by 48 · see citing works
Self-citationRohlfing, A. E., Eckenroth, B. E., Forster, E. R., Kevorkian, Y. L., Donnelly, M. L., de la Puebla, H. B., Doublié, S., & Shen, A. (2019) · PLoS Genetics · doi:10.1371/journal.pgen.1008224 · Cited by 48 · see citing works
The Metalloprotease ofListeria monocytogenesIs Activated by Intramolecular Autocatalysis
Bitar, A. P., Cao, M., & Marquis, H. (2007) · Journal of Bacteriology · doi:10.1128/jb.00852-07 · Cited by 47 · see citing works
Foophow, T., Tanaka, S., Angkawidjaja, C., Koga, Y., Takano, K., & Kanaya, S. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.05.064 · Cited by 44 · see citing works
Kinsella, R. L., Lopez, J., Palmer, L. D., Salinas, N. D., Skaar, E. P., Tolia, N. H., & Feldman, M. F. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.808394 · Cited by 44 · see citing works
“However, unlike elastase, which is produced as a preproelastase, where the prodomain functions as an intramolecular chaperone (30, 31), LipB and CpaB are encoded adjacently to their cognate effector proteins and are predicted to be membrane-bound.”
BackgroundA new approach for alteration of protease functions: pro-sequence engineering
Takagi, H., & Takahashi, M. (2003) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-003-1352-1 · Cited by 42 · see citing works
“Protein folding mediated by the pro-sequence is best understood in subtilisin, in particular subtilisin E of B. subtilis (Shinde and Inouye 2000).”
BackgroundKim, C. W., Han, K. S., Ryu, K., Kim, B. H., Kim, K., Choi, S. I., & Seong, B. L. (2007) · Protein Science · doi:10.1110/ps.062330907 · Cited by 42 · see citing works
“The N-terminal propeptides, usually polyanionic in nature (Jones et al. 2004), have been shown to directly assist the correct folding of their downstream proteins as intramolecular chaperones (Shinde and Inouye 2000).”
BackgroundSubbian, E., Yabuta, Y., & Shinde, U. P. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.01.028 · Cited by 42 · see citing works
Self-citationMultifunctional aspartic peptidase prosegments
Horimoto, Y., Dee, D. R., & Yada, R. Y. (2009) · New Biotechnology · doi:10.1016/j.nbt.2009.03.010 · Cited by 40 · see citing works
Reassembly of Active Caspase-3 Is Facilitated by the Propeptide
Feeney, B., & Clark, A. C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505834200 · Cited by 40 · see citing works
Wang, J., Wang, D., Wang, B., Mei, Z.-H., Liu, J., & Yu, H. (2012) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-012-4049-5 · Cited by 37 · see citing works
“They often function as intramolecular chaperones (IMCs) that facilitate protein folding (Shinde and Inouye 2000; 1993; Inouye 1991; Lee et al. 1991; Vandenhazel et al. 1993; Ikemura et al. 1987).”
BackgroundEffects of pre- and pro-sequence of thaumatin on the secretion by Pichia pastoris
Ide, N., Masuda, T., & Kitabatake, N. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.09.021 · Cited by 38 · see citing works
McIver, K. S. (2004) · Microbiology · doi:10.1099/mic.0.27340-0 · Cited by 38 · see citing works
“…serine proteinases (e.g. Saccharomyces cerevisiae carboxypeptidase Y and Yarrowia lipolytica alkaline extracellular protease), aspartic proteinases (e.g. S. cerevisiae proteinase A and Rhizopus niveus proteinase I) and thiol proteinases (e.g. cathepsins L and B) (reviewed by Shinde & Inouye, 2000).”
BackgroundGermond, J.-E., Delley, M., Gilbert, C., & Atlan, D. (2003) · Applied and Environmental Microbiology · doi:10.1128/aem.69.6.3377-3384.2003 · Cited by 36 · see citing works
“This prompted us to propose the prodomain of PrtB as a class I propeptide that confers a foldase activity sufficient for proteinase folding ( 34 ).”
BackgroundGoetting‐Minesky, M. P., Godovikova, V., & Fenno, J. C. (2021) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2021.668287 · Cited by 35 · see citing works
Rahman, M. M., Inoue, A., Tanaka, H., & Ojima, T. (2011) · Biochimie · doi:10.1016/j.biochi.2011.06.004 · Cited by 34 · see citing works
The pro‐peptide of proNGF: Structure formation and intramolecular association with NGF
Kliemannel, M., Golbik, R. P., Rudolph, R., Schwarz, E., & Lilie, H. (2007) · Protein Science · doi:10.1110/ps.062376207 · Cited by 33 · see citing works
“Copyright 2007 The Protein Society 411 Folding-promoting functions of pro-peptides have been reported for several proteins, which are expressed as (pre-)pro-proteins (Shinde and Inouye 2000).”
BackgroundSubbian, E., Yabuta, Y., & Shinde, U. P. (2004) · Biochemistry · doi:10.1021/bi048397x · Cited by 33 · see citing works
“This is consistent with extensive work on prokaryotic subtilisins and eukaryotic subtilisin/kexin-like prohormone convertases that emphasize the importance and necessity of propeptide domains in facilitating correct protein folding (11, 13).”
BackgroundSelf-citationCameron, A., Apletalina, E. V., & Lindberg, I. (2002) · The Enzymes · doi:10.1016/s1874-6047(02)80012-9 · Cited by 33 · see citing works
Folding Pathway Mediated by an Intramolecular Chaperone
Yabuta, Y., Subbian, E., Oiry, C., & Shinde, U. P. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212003200 · Cited by 32 · see citing works
Self-citationStructural Organization of Precursors of Thermolysin-like Proteinases
Demidyuk, I. V., Gasanov, E. V., Safina, D. R., & Kostrov, S. V. (2008) · The Protein Journal · doi:10.1007/s10930-008-9143-2 · Cited by 32 · see citing works
Pulido, M., Tanaka, S., Sringiew, C., You, D., Matsumura, H., Koga, Y., Takano, K., & Kanaya, S. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.10.030 · Cited by 31 · see citing works
Godlewska, M., Góra, M., Buckle, A. M., Porebski, B. T., Kemp, E. H., Sutton, B. J., Czarnocka, B., & Banga, J. P. (2013) · Thyroid · doi:10.1089/thy.2013.0127 · Cited by 31 · see citing works
“It is often observed that the intramolecular chaperone and the associated protein need not be covalently linked for correct chaperone function (57).”
Hailey, K. L., Li, S., Andersen, M. D., Roy, M., Woods, V. L., & Jennings, P. A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.027375 · Cited by 30 · see citing works
Pulido, M., Koga, Y., Takano, K., & Kanaya, S. (2007) · Protein Engineering Design and Selection · doi:10.1093/protein/gzm006 · Cited by 29 · see citing works
“The folding pathway of bacterial subtilisins has been most extensively studied for subtilisin E (Li et al., 1995; Fu et al., 2000; Shinde and Inouye, 2000; Yabuta et al., 2001; Yabuta et al., 2003; Subbian et al., 2005).”
BackgroundEndoproteolytic Cleavage of Human Thyroperoxidase
Fourn, V. L., Ferrand, M., & Franc, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408042200 · Cited by 28 · see citing works
Functional Roles of Furin in Cardio-Cerebrovascular Diseases
Wichaiyo, S., Koonyosying, P., & Morales, N. P. (2024) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.3c00325 · Cited by 27 · see citing works
Rahman, M. M., Wang, L., Inoue, A., & Ojima, T. (2012) · Carbohydrate Research · doi:10.1016/j.carres.2012.05.019 · Cited by 26 · see citing works
Dillon, S. L., Williamson, D. M., Elferich, J., Radler, D., Joshi, R., Thomas, G., & Shinde, U. P. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2012.06.023 · Cited by 26 · see citing works
Self-citationGrande, K. K., Gustin, J. K., Kessler, E., & Ohman, D. E. (2007) · Journal of Bacteriology · doi:10.1128/jb.01828-06 · Cited by 26 · see citing works
“A term that has been used to describe such a propeptide is intramolecular chaperone (IMC) ( 24 ).”
BackgroundLarsen, A. N., Moe, E., Helland, R., Gjellesvik, D. R., & Willassen, N. P. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.05044.x · Cited by 26 · see citing works
Khaitlina, S. Y., Bozhokina, E., Tsaplina, O. A., & Efremova, T. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21114025 · Cited by 25 · see citing works
“Similarly to other thermolysin-like proteases [27,28], protealysin is synthesized as a precursor containing a propeptide of about 50 amino acids that is removed during formation of mature active protein [29].”
BackgroundThe Mechanism by Which a Propeptide-encoded pH Sensor Regulates Spatiotemporal Activation of Furin
Williamson, D. M., Elferich, J., Ramakrishnan, P., Thomas, G., & Shinde, U. P. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.442681 · Cited by 25 · see citing works
Self-citationLiu, B., Zhang, J., Fang, Z., Du, G., Chen, J., & Liao, X. (2014) · Process Biochemistry · doi:10.1016/j.procbio.2014.04.021 · Cited by 25 · see citing works
Functional analysis of the propeptides of subtilisin E and aqualysin I as intramolecular chaperones
Takagi, H., Koga, M., Katsurada, S., Yabuta, Y., Shinde, U. P., Inouye, M., & Nakamori, S. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)03053-8 · Cited by 25 · see citing works
Self-citationPlíhal, O., Sklenář, J., Hofbauerová, K., Novák, P., Man, P., Pompach, P., Kavan, D., Ryšlavá, H., Weignerová, L., Charvátová-Pišvejcová, A., et al. (2007) · Biochemistry · doi:10.1021/bi061828m · Cited by 25 · see citing works
Gamble, M., Künze, G., Dodson, E. J., Wilson, K. S., & Jones, D. D. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1014229108 · Cited by 24 · see citing works
Uehara, R., Takeuchi, Y., Tanaka, S., Takano, K., Koga, Y., & Kanaya, S. (2012) · Biochemistry · doi:10.1021/bi300427u · Cited by 24 · see citing works
Ghosh, A., Chakrabarti, K., & Chattopadhyay, D. (2009) · Microbiology · doi:10.1099/mic.0.027573-0 · Cited by 23 · see citing works
Vévodová, J., Gamble, M., Künze, G., Ariza, A., Dodson, E. J., Jones, D. D., & Wilson, K. S. (2010) · Structure · doi:10.1016/j.str.2010.03.008 · Cited by 23 · see citing works
“This is in contrast to the kinetic stability observed for mature ESPs that compensates for their marginal thermodynamic stability (Bryan, 2002; Shinde and Inouye, 2000).”
BackgroundResultNA, B.-K., KANG, J.-M., Cheun, H., CHO, S.-H., MOON, S.-U., Kim, T.-S., & SOHN, W.-M. (2008) · Parasitology · doi:10.1017/s0031182008005350 · Cited by 22 · see citing works
“Although the pro-domain sequences of the enzymes are more variable than the mature domain, the two regions of pro-domain (ERFNIN and GNFD motifs) are relatively well-conserved and play an important role in the processing and folding of these enzymes (Smith and Gottesman, 1989; Vernet et al. 1995; Yamamoto et al. 1999;…”
BackgroundUehara, R., Angkawidjaja, C., Koga, Y., & Kanaya, S. (2013) · Biochemistry · doi:10.1021/bi401342k · Cited by 22 · see citing works
Substrate-induced activation of a trapped IMC-mediated protein folding intermediate.
Inouye, M., Fu, X., & Shinde, U. P. (2001) · Nature Structural Biology · doi:10.1038/86194 · Cited by 22 · see citing works
Self-citationBuczek, P., Buczek, O., & Bułaj, G. (2005) · Biopolymers · doi:10.1002/bip.20211 · Cited by 19 · see citing works
Jia, Y., Liu, H., Bao, W., Weng, M., Chen, W., Cai, Y., Zheng, Z., & Zou, G. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.11.011 · Cited by 21 · see citing works
Uehara, R., Ueda, Y., You, D., Koga, Y., & Kanaya, S. (2012) · FEBS Journal · doi:10.1111/febs.12091 · Cited by 20 · see citing works
Moroz, O. V., Blagova, E. V., Reiser, V., Saikia, R., Dalal, S., Jørgensen, C. I., Bhatia, V. K., Baunsgaard, L., Andersen, B., Svendsen, A., et al. (2019) · ACS Omega · doi:10.1021/acsomega.9b00612 · Cited by 20 · see citing works
Fukada, K., Inoue, T., & Shiraishi, H. (2006) · The Plant Cell · doi:10.1105/tpc.106.041343 · Cited by 18 · see citing works
“Since the amino acid sequence of prosequences among homologous proteases is less conserved than protease domains (Shinde and Inouye, 2000), it is difficult to predict the role of the prosequence from the amino acid sequence in the function of VheA.”
BackgroundAutotomic Behavior of the Propeptide in Propeptide-mediated Folding of Prosubtilisin E
Falzon, L., Patel, S. S., Chen, Y.-J., & Inouye, M. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.11.019 · Cited by 17 · see citing works
Self-citationMolecular and Biochemical Properties of a Cysteine Protease of Acanthamoeba castellanii
Hong, Y., Kang, J., Joo, S.-Y., Song, S., Lê, H. G., Thái, T. L., Lee, J., Goo, Y., Chung, D.-I., Sohn, W., et al. (2018) · Korean Journal of Parasitology · doi:10.3347/kjp.2018.56.5.409 · Cited by 16 · see citing works
“The ERFNIN and GNFD motifs, which are well-conserved and play an important role in the processing and folding of cathepsin L family cysteine proteases [28,29], are well conserved in the pre-prodomain of AcCP.”
BackgroundGamble, M., Künze, G., Brancale, A., Wilson, K. S., & Jones, D. D. (2012) · FEBS Open Bio · doi:10.1016/j.fob.2012.07.001 · Cited by 15 · see citing works
“Given that they are active within the cell, little is known about substrate specificity and the role of stress signals such as divalent metal ions in modulating ISP function.”
BackgroundRecombinant prosegment peptide acts as a folding catalyst and inhibitor of native pepsin
Dee, D. R., Filonowicz, S., Horimoto, Y., & Yada, R. Y. (2009) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2009.08.017 · Cited by 15 · see citing works
Bronsoms, S., Villanueva, J., Canals, F., Querol, E., & Avilés, F. X. (2003) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2003.03754.x · Cited by 15 · see citing works
O'Neil, H. S., Forster, B. M., Roberts, K. L., Chambers, A. J., Bitar, A. P., & Marquis, H. (2009) · Journal of Bacteriology · doi:10.1128/jb.01168-08 · Cited by 14 · see citing works
“Propeptides often function as intramolecular chaperones catalyzing the folding of their covalently bound protease ( 30 ).”
BackgroundInfluentialŠkerlová, J., Bláha, J., Pachl, P., Hofbauerová, K., Kukačka, Z., Man, P., Pompach, P., Novák, P., Otwinowski, Z., Brynda, J., et al. (2017) · FEBS Journal · doi:10.1111/febs.14360 · Cited by 14 · see citing works
Li, K., Zhu, Y., Yan, W., Deng, X., Xiao, Y., Song, L., Fang, R., Jia, Y., & Tang, X. (2019) · PLoS Pathogens · doi:10.1371/journal.ppat.1007673 · Cited by 14 · see citing works
Yeh, C., HUANG, X.-H., & Sue, C.-W. (2008) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf801580s · Cited by 14 · see citing works
López-Fernández, J., Benaiges, M. D., & Valero, F. (2021) · Catalysts · doi:10.3390/catal11101192 · Cited by 13 · see citing works
“Obtaining the mature form of the lipase (rROL) entails removing the presequence and prosequence [10,11].”
BackgroundWang, Z., Lv, P., Luo, W., Yuan, Z., & Dong, H. (2016) · The Journal of General and Applied Microbiology · doi:10.2323/jgam.62.25 · Cited by 13 · see citing works
“Propeptide regions often function as IMCs which facilitate protein folding (Shinde and Inouye, 2000).”
BackgroundDai, Z., Fu, H., Zhang, Y., Zeng, J., Tang, B., & Tang, X. (2012) · Applied and Environmental Microbiology · doi:10.1128/aem.00548-12 · Cited by 13 · see citing works
“The N-terminal propeptides of bacterial subtilases usually function as intramolecular chaperones to assist the correct folding of the catalytic domain and as potent inhibitors of the mature enzyme (26, 27); however, the Pls N N-terminal propeptide deletion mutant displayed proteolytic activity in the gelatin overlay a…”
BackgroundInfluentialpH-Dependent Activation of Streptomyces hygroscopicus Transglutaminase Mediated by Intein
Du, K., Liu, Z., Cui, W., Zhou, L., Liu, Y., Du, G., Chen, J., & Zhou, Z. (2013) · Applied and Environmental Microbiology · doi:10.1128/aem.02820-13 · Cited by 12 · see citing works
“The proregion is essential for efficient protein folding and the suppression of mature enzyme activity (2).”
BackgroundHong, T., Pan, R., Ke, J., Luo, Y., Hao, Y., Chen, L., Tu, D., Dai, Y., Chen, T., & Chen, S. (2023) · Brazilian Journal of Microbiology · doi:10.1007/s42770-023-01114-y · Cited by 11 · see citing works
“Most of their mature enzymes contain a catalytic domain, and a few also contain a C-terminal region [46, 47].”
BackgroundConformational analyses of a partially‐folded bioactive prodomain of human furin
Bhattacharjya, S., Xu, P., Wang, P., Osborne, M. J., & Ni, F. (2007) · Biopolymers · doi:10.1002/bip.20748 · Cited by 11 · see citing works
Four residues of propeptide are essential for precursor folding of nattokinase
Jia, Y., Cao, X., Deng, Y., Bao, W., Tang, C., Ding, H., Zheng, Z., & Zou, G. (2014) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmu093 · Cited by 10 · see citing works
“Unlike molecular chaperone, the IMC is encoded in the primary sequence of the protein and is usually termed a propeptide.”
BackgroundInfluentialSynthesis of functionalized furopyrazines as restricted dipeptidomimetics
Claerhout, S., Sharma, S., Sköld, C., Cavalluzzo, C., Sandström, A., Larhed, M., Thirumal, M., Parmar, V. S., & der Eycken, E. V. V. (2012) · Tetrahedron · doi:10.1016/j.tet.2012.02.022 · Cited by 10 · see citing works
Shewasin A, an active pepsin homolog from the bacterium Shewanella amazonensis
Simões, I., Faro, R., Bur, D., Kay, J., & Faro, C. (2011) · FEBS Journal · doi:10.1111/j.1742-4658.2011.08243.x · Cited by 10 · see citing works
Kouwen, T. R. H. M., Nielsen, A. K., Denham, E. L., Dubois, J. F., Dorenbos, R., Rasmussen, M., Quax, W. J., Freudl, R., & van Dijl, J. M. (2009) · Applied and Environmental Microbiology · doi:10.1128/aem.01671-09 · Cited by 10 · see citing works
“cell envelope after translocation (46, 49, 51, 61).”
BackgroundUehara, R., Tanaka, S., Takano, K., Koga, Y., & Kanaya, S. (2012) · Extremophiles · doi:10.1007/s00792-012-0479-3 · Cited by 9 · see citing works
Donnelly, M. L., Forster, E. R., Rohlfing, A. E., & Shen, A. (2020) · Biochemical Journal · doi:10.1042/bcj20190875 · Cited by 8 · see citing works
- Authors
- Shinde, U., & Inouye, M.
- Venue
- Seminars in Cell & Developmental Biology
- Publisher
- Elsevier BV
- Published
- 2000-02
- Volume
- 11
- Issue
- 1
- Pages
- 35-44
- ISSN
- 1084-9521 (ISSN-L)
- OpenAlex
- W1998330911
- Cited by
- 141
- References
- 98
- Citations by year
- 2025: 2 · 2024: 3 · 2023: 3 · 2021: 4 · 2020: 5 · 2019: 3 · 2018: 1 · 2017: 3 · 2016: 3 · 2015: 2 · 2014: 3 · 2013: 7 · 2012: 12
- FWCI
- 2.65
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Seminars in Cell and Developmental Biology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
- Keywords
- intramolecular chaperone, propeptide, protein folding, signal peptide, proprotein processing, post-translational regulation, protein oligomerization, protein localization, enzyme activity modulation, protein stability
- MeSH terms
- Animals, Cell Physiological Phenomena, Humans, Models, Biological, Peptides, Protein Folding, Molecular Chaperones
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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